Crystal structure of the soluble form of the redox-regulated chloride ion channel protein CLIC4.
Identifieur interne : 000E20 ( Main/Exploration ); précédent : 000E19; suivant : 000E21Crystal structure of the soluble form of the redox-regulated chloride ion channel protein CLIC4.
Auteurs : Dene R. Littler [Australie] ; Nagi N. Assaad ; Stephen J. Harrop ; Louise J. Brown ; Greg J. Pankhurst ; Paolo Luciani ; Marie-Isabel Aguilar ; Michele Mazzanti ; Mark A. Berryman ; Samuel N. Breit ; Paul M G. CurmiSource :
- The FEBS journal [ 1742-464X ] ; 2005.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Canaux chlorure (composition chimique), Canaux chlorure (métabolisme), Chlorures (métabolisme), Cristallographie aux rayons X (MeSH), Données de séquences moléculaires (MeSH), Humains (MeSH), Liposomes (métabolisme), Modèles moléculaires (MeSH), Oxydoréduction (MeSH), Similitude structurale de protéines (MeSH), Solubilité (MeSH), Structure tertiaire des protéines (MeSH), Séquence d'acides aminés (MeSH), Techniques de patch-clamp (MeSH), Électrophysiologie (MeSH).
- MESH :
- composition chimique : Canaux chlorure.
- métabolisme : Canaux chlorure, Chlorures, Liposomes.
- Alignement de séquences, Cristallographie aux rayons X, Données de séquences moléculaires, Humains, Modèles moléculaires, Oxydoréduction, Similitude structurale de protéines, Solubilité, Structure tertiaire des protéines, Séquence d'acides aminés, Techniques de patch-clamp, Électrophysiologie.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Chloride Channels (chemistry), Chloride Channels (metabolism), Chlorides (metabolism), Crystallography, X-Ray (MeSH), Electrophysiology (MeSH), Humans (MeSH), Liposomes (metabolism), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Oxidation-Reduction (MeSH), Patch-Clamp Techniques (MeSH), Protein Structure, Tertiary (MeSH), Sequence Alignment (MeSH), Solubility (MeSH), Structural Homology, Protein (MeSH).
- MESH :
- chemical , chemistry : Chloride Channels.
- chemical , metabolism : Chloride Channels, Chlorides, Liposomes.
- Amino Acid Sequence, Crystallography, X-Ray, Electrophysiology, Humans, Models, Molecular, Molecular Sequence Data, Oxidation-Reduction, Patch-Clamp Techniques, Protein Structure, Tertiary, Sequence Alignment, Solubility, Structural Homology, Protein.
Abstract
The structure of CLIC4, a member of the CLIC family of putative intracellular chloride ion channel proteins, has been determined at 1.8 Angstroms resolution by X-ray crystallography. The protein is monomeric and it is structurally similar to CLIC1, belonging to the GST fold class. Differences between the structures of CLIC1 and CLIC4 are localized to helix 2 in the glutaredoxin-like N-terminal domain, which has previously been shown to undergo a dramatic structural change in CLIC1 upon oxidation. The structural differences in this region correlate with the sequence differences, where the CLIC1 sequence appears to be atypical of the family. Purified, recombinant, wild-type CLIC4 is shown to bind to artificial lipid bilayers, induce a chloride efflux current when associated with artificial liposomes and produce an ion channel in artificial bilayers with a conductance of 30 pS. Membrane binding is enhanced by oxidation of CLIC4 while no channels were observed via tip-dip electrophysiology in the presence of a reducing agent. Thus, recombinant CLIC4 appears to be able to form a redox-regulated ion channel in the absence of any partner proteins.
DOI: 10.1111/j.1742-4658.2005.04909.x
PubMed: 16176272
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Harrop</name></author><author><name sortKey="Brown, Louise J" sort="Brown, Louise J" uniqKey="Brown L" first="Louise J" last="Brown">Louise J. Brown</name></author><author><name sortKey="Pankhurst, Greg J" sort="Pankhurst, Greg J" uniqKey="Pankhurst G" first="Greg J" last="Pankhurst">Greg J. Pankhurst</name></author><author><name sortKey="Luciani, Paolo" sort="Luciani, Paolo" uniqKey="Luciani P" first="Paolo" last="Luciani">Paolo Luciani</name></author><author><name sortKey="Aguilar, Marie Isabel" sort="Aguilar, Marie Isabel" uniqKey="Aguilar M" first="Marie-Isabel" last="Aguilar">Marie-Isabel Aguilar</name></author><author><name sortKey="Mazzanti, Michele" sort="Mazzanti, Michele" uniqKey="Mazzanti M" first="Michele" last="Mazzanti">Michele Mazzanti</name></author><author><name sortKey="Berryman, Mark A" sort="Berryman, Mark A" uniqKey="Berryman M" first="Mark A" last="Berryman">Mark A. 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Littler</name><affiliation wicri:level="3"><nlm:affiliation>School of Physics, University of New South Wales, Sydney, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>School of Physics, University of New South Wales, Sydney</wicri:regionArea><placeName><settlement type="city">Sydney</settlement><region type="état">Nouvelle-Galles du Sud</region></placeName></affiliation></author><author><name sortKey="Assaad, Nagi N" sort="Assaad, Nagi N" uniqKey="Assaad N" first="Nagi N" last="Assaad">Nagi N. Assaad</name></author><author><name sortKey="Harrop, Stephen J" sort="Harrop, Stephen J" uniqKey="Harrop S" first="Stephen J" last="Harrop">Stephen J. Harrop</name></author><author><name sortKey="Brown, Louise J" sort="Brown, Louise J" uniqKey="Brown L" first="Louise J" last="Brown">Louise J. Brown</name></author><author><name sortKey="Pankhurst, Greg J" sort="Pankhurst, Greg J" uniqKey="Pankhurst G" first="Greg J" last="Pankhurst">Greg J. Pankhurst</name></author><author><name sortKey="Luciani, Paolo" sort="Luciani, Paolo" uniqKey="Luciani P" first="Paolo" last="Luciani">Paolo Luciani</name></author><author><name sortKey="Aguilar, Marie Isabel" sort="Aguilar, Marie Isabel" uniqKey="Aguilar M" first="Marie-Isabel" last="Aguilar">Marie-Isabel Aguilar</name></author><author><name sortKey="Mazzanti, Michele" sort="Mazzanti, Michele" uniqKey="Mazzanti M" first="Michele" last="Mazzanti">Michele Mazzanti</name></author><author><name sortKey="Berryman, Mark A" sort="Berryman, Mark A" uniqKey="Berryman M" first="Mark A" last="Berryman">Mark A. Berryman</name></author><author><name sortKey="Breit, Samuel N" sort="Breit, Samuel N" uniqKey="Breit S" first="Samuel N" last="Breit">Samuel N. Breit</name></author><author><name sortKey="Curmi, Paul M G" sort="Curmi, Paul M G" uniqKey="Curmi P" first="Paul M G" last="Curmi">Paul M G. Curmi</name></author></analytic><series><title level="j">The FEBS journal</title><idno type="ISSN">1742-464X</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Chloride Channels (chemistry)</term><term>Chloride Channels (metabolism)</term><term>Chlorides (metabolism)</term><term>Crystallography, X-Ray (MeSH)</term><term>Electrophysiology (MeSH)</term><term>Humans (MeSH)</term><term>Liposomes (metabolism)</term><term>Models, Molecular (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Patch-Clamp Techniques (MeSH)</term><term>Protein Structure, Tertiary (MeSH)</term><term>Sequence Alignment (MeSH)</term><term>Solubility (MeSH)</term><term>Structural Homology, Protein (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term><term>Canaux chlorure (composition chimique)</term><term>Canaux chlorure (métabolisme)</term><term>Chlorures (métabolisme)</term><term>Cristallographie aux rayons X (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Humains (MeSH)</term><term>Liposomes (métabolisme)</term><term>Modèles moléculaires (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Similitude structurale de protéines (MeSH)</term><term>Solubilité (MeSH)</term><term>Structure tertiaire des protéines (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Techniques de patch-clamp (MeSH)</term><term>Électrophysiologie (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Chloride Channels</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Chloride Channels</term><term>Chlorides</term><term>Liposomes</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Canaux chlorure</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Canaux chlorure</term><term>Chlorures</term><term>Liposomes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Crystallography, X-Ray</term><term>Electrophysiology</term><term>Humans</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Oxidation-Reduction</term><term>Patch-Clamp Techniques</term><term>Protein Structure, Tertiary</term><term>Sequence Alignment</term><term>Solubility</term><term>Structural Homology, Protein</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Cristallographie aux rayons X</term><term>Données de séquences moléculaires</term><term>Humains</term><term>Modèles moléculaires</term><term>Oxydoréduction</term><term>Similitude structurale de protéines</term><term>Solubilité</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term><term>Techniques de patch-clamp</term><term>Électrophysiologie</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The structure of CLIC4, a member of the CLIC family of putative intracellular chloride ion channel proteins, has been determined at 1.8 Angstroms resolution by X-ray crystallography. The protein is monomeric and it is structurally similar to CLIC1, belonging to the GST fold class. Differences between the structures of CLIC1 and CLIC4 are localized to helix 2 in the glutaredoxin-like N-terminal domain, which has previously been shown to undergo a dramatic structural change in CLIC1 upon oxidation. The structural differences in this region correlate with the sequence differences, where the CLIC1 sequence appears to be atypical of the family. Purified, recombinant, wild-type CLIC4 is shown to bind to artificial lipid bilayers, induce a chloride efflux current when associated with artificial liposomes and produce an ion channel in artificial bilayers with a conductance of 30 pS. Membrane binding is enhanced by oxidation of CLIC4 while no channels were observed via tip-dip electrophysiology in the presence of a reducing agent. Thus, recombinant CLIC4 appears to be able to form a redox-regulated ion channel in the absence of any partner proteins.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16176272</PMID><DateCompleted><Year>2005</Year><Month>11</Month><Day>14</Day></DateCompleted><DateRevised><Year>2006</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1742-464X</ISSN><JournalIssue CitedMedium="Print"><Volume>272</Volume><Issue>19</Issue><PubDate><Year>2005</Year><Month>Oct</Month></PubDate></JournalIssue><Title>The FEBS journal</Title><ISOAbbreviation>FEBS J</ISOAbbreviation></Journal><ArticleTitle>Crystal structure of the soluble form of the redox-regulated chloride ion channel protein CLIC4.</ArticleTitle><Pagination><MedlinePgn>4996-5007</MedlinePgn></Pagination><Abstract><AbstractText>The structure of CLIC4, a member of the CLIC family of putative intracellular chloride ion channel proteins, has been determined at 1.8 Angstroms resolution by X-ray crystallography. The protein is monomeric and it is structurally similar to CLIC1, belonging to the GST fold class. Differences between the structures of CLIC1 and CLIC4 are localized to helix 2 in the glutaredoxin-like N-terminal domain, which has previously been shown to undergo a dramatic structural change in CLIC1 upon oxidation. The structural differences in this region correlate with the sequence differences, where the CLIC1 sequence appears to be atypical of the family. Purified, recombinant, wild-type CLIC4 is shown to bind to artificial lipid bilayers, induce a chloride efflux current when associated with artificial liposomes and produce an ion channel in artificial bilayers with a conductance of 30 pS. Membrane binding is enhanced by oxidation of CLIC4 while no channels were observed via tip-dip electrophysiology in the presence of a reducing agent. Thus, recombinant CLIC4 appears to be able to form a redox-regulated ion channel in the absence of any partner proteins.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Littler</LastName><ForeName>Dene R</ForeName><Initials>DR</Initials><AffiliationInfo><Affiliation>School of Physics, University of New South Wales, Sydney, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Assaad</LastName><ForeName>Nagi N</ForeName><Initials>NN</Initials></Author><Author ValidYN="Y"><LastName>Harrop</LastName><ForeName>Stephen J</ForeName><Initials>SJ</Initials></Author><Author ValidYN="Y"><LastName>Brown</LastName><ForeName>Louise J</ForeName><Initials>LJ</Initials></Author><Author ValidYN="Y"><LastName>Pankhurst</LastName><ForeName>Greg J</ForeName><Initials>GJ</Initials></Author><Author ValidYN="Y"><LastName>Luciani</LastName><ForeName>Paolo</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Aguilar</LastName><ForeName>Marie-Isabel</ForeName><Initials>MI</Initials></Author><Author ValidYN="Y"><LastName>Mazzanti</LastName><ForeName>Michele</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Berryman</LastName><ForeName>Mark A</ForeName><Initials>MA</Initials></Author><Author ValidYN="Y"><LastName>Breit</LastName><ForeName>Samuel N</ForeName><Initials>SN</Initials></Author><Author ValidYN="Y"><LastName>Curmi</LastName><ForeName>Paul M G</ForeName><Initials>PM</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>FEBS J</MedlineTA><NlmUniqueID>101229646</NlmUniqueID><ISSNLinking>1742-464X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C086321">CLC-1 channel</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C484312">CLCN4 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018118">Chloride Channels</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002712">Chlorides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008081">Liposomes</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018118" MajorTopicYN="N">Chloride Channels</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002712" MajorTopicYN="N">Chlorides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004594" MajorTopicYN="N">Electrophysiology</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008081" MajorTopicYN="N">Liposomes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018408" MajorTopicYN="N">Patch-Clamp Techniques</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012995" MajorTopicYN="N">Solubility</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D040681" MajorTopicYN="N">Structural Homology, Protein</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2005</Year><Month>9</Month><Day>24</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2005</Year><Month>11</Month><Day>15</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2005</Year><Month>9</Month><Day>24</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">16176272</ArticleId><ArticleId IdType="pii">EJB4909</ArticleId><ArticleId IdType="doi">10.1111/j.1742-4658.2005.04909.x</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Australie</li></country><region><li>Nouvelle-Galles du Sud</li></region><settlement><li>Sydney</li></settlement></list><tree><noCountry><name sortKey="Aguilar, Marie Isabel" sort="Aguilar, Marie Isabel" uniqKey="Aguilar M" first="Marie-Isabel" last="Aguilar">Marie-Isabel Aguilar</name><name sortKey="Assaad, Nagi N" sort="Assaad, Nagi N" uniqKey="Assaad N" first="Nagi N" last="Assaad">Nagi N. Assaad</name><name sortKey="Berryman, Mark A" sort="Berryman, Mark A" uniqKey="Berryman M" first="Mark A" last="Berryman">Mark A. Berryman</name><name sortKey="Breit, Samuel N" sort="Breit, Samuel N" uniqKey="Breit S" first="Samuel N" last="Breit">Samuel N. Breit</name><name sortKey="Brown, Louise J" sort="Brown, Louise J" uniqKey="Brown L" first="Louise J" last="Brown">Louise J. Brown</name><name sortKey="Curmi, Paul M G" sort="Curmi, Paul M G" uniqKey="Curmi P" first="Paul M G" last="Curmi">Paul M G. Curmi</name><name sortKey="Harrop, Stephen J" sort="Harrop, Stephen J" uniqKey="Harrop S" first="Stephen J" last="Harrop">Stephen J. Harrop</name><name sortKey="Luciani, Paolo" sort="Luciani, Paolo" uniqKey="Luciani P" first="Paolo" last="Luciani">Paolo Luciani</name><name sortKey="Mazzanti, Michele" sort="Mazzanti, Michele" uniqKey="Mazzanti M" first="Michele" last="Mazzanti">Michele Mazzanti</name><name sortKey="Pankhurst, Greg J" sort="Pankhurst, Greg J" uniqKey="Pankhurst G" first="Greg J" last="Pankhurst">Greg J. Pankhurst</name></noCountry><country name="Australie"><region name="Nouvelle-Galles du Sud"><name sortKey="Littler, Dene R" sort="Littler, Dene R" uniqKey="Littler D" first="Dene R" last="Littler">Dene R. Littler</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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