SgmlV1, Main, Exploration, bibRecord, 002D58

The Three-dimensional Solution Structure of Human Stefin A

Identifieur interne : 002D58 ( Main/Exploration ); précédent : 002D57; suivant : 002D59

The Three-dimensional Solution Structure of Human Stefin A

Auteurs : John R. Martin [Royaume-Uni] ; Jeremy C. Craven [Royaume-Uni] ; Roman Jerala [Slovénie] ; Louise Kroon-Žitko [Slovénie] ; Eva Žerovnik [Slovénie] ; Vito Turk [Slovénie] ; Jonathan P. Waltho [Royaume-Uni]

Source :

Journal of Molecular Biology [ 0022-2836 ] ; 1995.

RBID : ISTEX:B067B0F1FAAA2AA83A2DF15AB7F12D1AC76B84C7

English descriptors

Abstract

Abstract: The three-dimensional solution structure of recombinant human stefin A has been determined by a simulated annealing protocol using a total of 1113 distance and angle constraints obtained from1H and15N HMR spectroscopy. The solution structure is represented by a family of 17 conformers with an average root-mean-square deviation relative to the mean structure of 0.44 Å for backbone atoms and 0.94 Å for all heavy atoms for the main body of the structure. The protein has a well-defined global fold consisting of five anti-parallel β-strands wrapped around a central five-turn α-helix. There is considerable similarity between the structural features of free stefin A in solution and the X-ray structure of the homologous protein stefin B in its complex with papain, but there are also some important differences in the regions which are fundamental to proteinase binding. The differences consist primarily of two regions of high conformational heterogeneity in free stefin A which correspond in stefin B to two of the components of the tripartite wedge that docks into the active site of the target proteinase. These regions, which are shown to be mobile in solution, are the five N-terminal residues and the second binding loop. In the bound conformation of stefin B they form a turn and a short helix, respectively.

Url:

https://api.istex.fr/ark:/67375/6H6-5313XTHB-Q/fulltext.pdf

DOI: 10.1006/jmbi.1994.0088

Affiliations:

Royaume-Uni, Slovénie

Links toward previous steps (curation, corpus...)

to stream Istex, to step Corpus: 002D53
to stream Istex, to step Curation: 002365
to stream Istex, to step Checkpoint: 002879
to stream Main, to step Merge: 002F26
to stream Main, to step Curation: 002D58

Le document en format XML

<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">The Three-dimensional Solution Structure of Human Stefin A</title>
<author><name sortKey="Martin, John R" sort="Martin, John R" uniqKey="Martin J" first="John R." last="Martin">John R. Martin</name>
</author>
<author><name sortKey="Craven, Jeremy C" sort="Craven, Jeremy C" uniqKey="Craven J" first="Jeremy C." last="Craven">Jeremy C. Craven</name>
</author>
<author><name sortKey="Jerala, Roman" sort="Jerala, Roman" uniqKey="Jerala R" first="Roman" last="Jerala">Roman Jerala</name>
</author>
<author><name sortKey="Kroon Itko, Louise" sort="Kroon Itko, Louise" uniqKey="Kroon Itko L" first="Louise" last="Kroon-Žitko">Louise Kroon-Žitko</name>
</author>
<author><name sortKey="Zerovnik, Eva" sort="Zerovnik, Eva" uniqKey="Zerovnik E" first="Eva" last="Žerovnik">Eva Žerovnik</name>
</author>
<author><name sortKey="Turk, Vito" sort="Turk, Vito" uniqKey="Turk V" first="Vito" last="Turk">Vito Turk</name>
</author>
<author><name sortKey="Waltho, Jonathan P" sort="Waltho, Jonathan P" uniqKey="Waltho J" first="Jonathan P." last="Waltho">Jonathan P. Waltho</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">ISTEX</idno>
<idno type="RBID">ISTEX:B067B0F1FAAA2AA83A2DF15AB7F12D1AC76B84C7</idno>
<date when="1995" year="1995">1995</date>
<idno type="doi">10.1006/jmbi.1994.0088</idno>
<idno type="url">https://api.istex.fr/ark:/67375/6H6-5313XTHB-Q/fulltext.pdf</idno>
<idno type="wicri:Area/Istex/Corpus">002D53</idno>
<idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">002D53</idno>
<idno type="wicri:Area/Istex/Curation">002365</idno>
<idno type="wicri:Area/Istex/Checkpoint">002879</idno>
<idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">002879</idno>
<idno type="wicri:doubleKey">0022-2836:1995:Martin J:the:three:dimensional</idno>
<idno type="wicri:Area/Main/Merge">002F26</idno>
<idno type="wicri:Area/Main/Curation">002D58</idno>
<idno type="wicri:Area/Main/Exploration">002D58</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">The Three-dimensional Solution Structure of Human Stefin A</title>
<author><name sortKey="Martin, John R" sort="Martin, John R" uniqKey="Martin J" first="John R." last="Martin">John R. Martin</name>
<affiliation wicri:level="1"><country xml:lang="fr">Royaume-Uni</country>
<wicri:regionArea>Krebs Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, P.O. Box 594, Sheffield, S10 2UH</wicri:regionArea>
<wicri:noRegion>S10 2UH</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Craven, Jeremy C" sort="Craven, Jeremy C" uniqKey="Craven J" first="Jeremy C." last="Craven">Jeremy C. Craven</name>
<affiliation wicri:level="1"><country xml:lang="fr">Royaume-Uni</country>
<wicri:regionArea>Krebs Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, P.O. Box 594, Sheffield, S10 2UH</wicri:regionArea>
<wicri:noRegion>S10 2UH</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Jerala, Roman" sort="Jerala, Roman" uniqKey="Jerala R" first="Roman" last="Jerala">Roman Jerala</name>
<affiliation wicri:level="1"><country xml:lang="fr">Slovénie</country>
<wicri:regionArea>Department of Biochemistry and Molecular Biology, Jožet Stefan Institute, Jamova 39, 6100, Ljubljana</wicri:regionArea>
<wicri:noRegion>Ljubljana</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Kroon Itko, Louise" sort="Kroon Itko, Louise" uniqKey="Kroon Itko L" first="Louise" last="Kroon-Žitko">Louise Kroon-Žitko</name>
<affiliation wicri:level="1"><country xml:lang="fr">Slovénie</country>
<wicri:regionArea>Department of Biochemistry and Molecular Biology, Jožet Stefan Institute, Jamova 39, 6100, Ljubljana</wicri:regionArea>
<wicri:noRegion>Ljubljana</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Zerovnik, Eva" sort="Zerovnik, Eva" uniqKey="Zerovnik E" first="Eva" last="Žerovnik">Eva Žerovnik</name>
<affiliation wicri:level="1"><country xml:lang="fr">Slovénie</country>
<wicri:regionArea>Department of Biochemistry and Molecular Biology, Jožet Stefan Institute, Jamova 39, 6100, Ljubljana</wicri:regionArea>
<wicri:noRegion>Ljubljana</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Turk, Vito" sort="Turk, Vito" uniqKey="Turk V" first="Vito" last="Turk">Vito Turk</name>
<affiliation wicri:level="1"><country xml:lang="fr">Slovénie</country>
<wicri:regionArea>Department of Biochemistry and Molecular Biology, Jožet Stefan Institute, Jamova 39, 6100, Ljubljana</wicri:regionArea>
<wicri:noRegion>Ljubljana</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Waltho, Jonathan P" sort="Waltho, Jonathan P" uniqKey="Waltho J" first="Jonathan P." last="Waltho">Jonathan P. Waltho</name>
<affiliation wicri:level="1"><country xml:lang="fr">Royaume-Uni</country>
<wicri:regionArea>Krebs Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, P.O. Box 594, Sheffield, S10 2UH</wicri:regionArea>
<wicri:noRegion>S10 2UH</wicri:noRegion>
</affiliation>
</author>
</analytic>
<monogr></monogr>
<series><title level="j">Journal of Molecular Biology</title>
<title level="j" type="abbrev">YJMBI</title>
<idno type="ISSN">0022-2836</idno>
<imprint><publisher>ELSEVIER</publisher>
<date type="published" when="1995">1995</date>
<biblScope unit="volume">246</biblScope>
<biblScope unit="issue">2</biblScope>
<biblScope unit="page" from="331">331</biblScope>
<biblScope unit="page" to="343">343</biblScope>
</imprint>
<idno type="ISSN">0022-2836</idno>
</series>
</biblStruct>
</sourceDesc>
<seriesStmt><idno type="ISSN">0022-2836</idno>
</seriesStmt>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>cystatins</term>
<term>protein NMR structure</term>
<term>protein dynamics</term>
<term>protein–protein interactions</term>
<term>stefins</term>
</keywords>
<keywords scheme="Teeft" xml:lang="en"><term>Acta</term>
<term>Acta histochem</term>
<term>Active site</term>
<term>Amide</term>
<term>Amide proton</term>
<term>Amide protons</term>
<term>Annealing protocol</term>
<term>Average structure</term>
<term>Average unit vector</term>
<term>Backbone</term>
<term>Backbone atoms</term>
<term>Backbone carbonyl oxygen</term>
<term>Backbone torsional angles</term>
<term>Barrett</term>
<term>Binding energy</term>
<term>Binding loop</term>
<term>Binding regions</term>
<term>Biol</term>
<term>Calibration curve</term>
<term>Carbonyl</term>
<term>Catalytic residue</term>
<term>Chem</term>
<term>Chicken cystatin</term>
<term>Complex formation</term>
<term>Conformation</term>
<term>Conformational</term>
<term>Conformational space</term>
<term>Considerable similarity</term>
<term>Constraint</term>
<term>Convex face</term>
<term>Core repulsion</term>
<term>Core repulsion force</term>
<term>Crystal structure</term>
<term>Cystatin</term>
<term>Cystatin family</term>
<term>Cystatin superfamily</term>
<term>Cystatins</term>
<term>Cysteine</term>
<term>Cysteine proteinase inhibitors</term>
<term>Cysteine proteinases</term>
<term>Dihedral angle constraints</term>
<term>Distance constraints</term>
<term>Distance data</term>
<term>Distance limits</term>
<term>Disulphide bonds</term>
<term>Early part</term>
<term>Energy minimisation</term>
<term>Epidermal inhibitor</term>
<term>Febs letters</term>
<term>Form hydrogen bonds</term>
<term>Free inhibitor</term>
<term>Good sampling</term>
<term>Hairpin loop</term>
<term>Heavy atoms</term>
<term>Helix</term>
<term>High degree</term>
<term>High values</term>
<term>Human neoplasms</term>
<term>Hydrogen bond</term>
<term>Hydrogen bond acceptor</term>
<term>Hydrogen bond constraints</term>
<term>Hydrogen bonds</term>
<term>Hydroxyl</term>
<term>Hydroxyl group</term>
<term>Inhibitor</term>
<term>Inhibitory</term>
<term>Interproton distances</term>
<term>Isopropyl group</term>
<term>Jarvinen</term>
<term>Jerala</term>
<term>Krebs institute</term>
<term>Large difference</term>
<term>Least squares</term>
<term>Less regions</term>
<term>Long range</term>
<term>Long range noes</term>
<term>Machleidt</term>
<term>Main body</term>
<term>Medium range</term>
<term>Model structure</term>
<term>Molecular mass</term>
<term>Noesy spectra</term>
<term>Overall correlation time</term>
<term>Papain</term>
<term>Primary helix</term>
<term>Protein chem</term>
<term>Protein inhibitors</term>
<term>Protein structures</term>
<term>Proteinase</term>
<term>Proteinase binding</term>
<term>Proton</term>
<term>Quantum coherence</term>
<term>Recombinant</term>
<term>Residue</term>
<term>Rinne</term>
<term>Second binding loop</term>
<term>Secondary structure</term>
<term>Sequence identity</term>
<term>Sequential</term>
<term>Short distances</term>
<term>Single conformation</term>
<term>Solution structure</term>
<term>Solution structures</term>
<term>Solvent exposure</term>
<term>Spectroscopy</term>
<term>Squamous epithelia</term>
<term>Strand</term>
<term>Strand results</term>
<term>Structure calculation protocol</term>
<term>Structure calculations</term>
<term>Stubbs</term>
<term>Target proteinase</term>
<term>Thermal denaturation</term>
<term>Torsional</term>
<term>Torsional angles</term>
<term>Transverse relaxation times</term>
<term>Tripartite wedge</term>
<term>Vector order parameter</term>
</keywords>
</textClass>
<langUsage><language ident="en">en</language>
</langUsage>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Abstract: The three-dimensional solution structure of recombinant human stefin A has been determined by a simulated annealing protocol using a total of 1113 distance and angle constraints obtained from1H and15N HMR spectroscopy. The solution structure is represented by a family of 17 conformers with an average root-mean-square deviation relative to the mean structure of 0.44 Å for backbone atoms and 0.94 Å for all heavy atoms for the main body of the structure. The protein has a well-defined global fold consisting of five anti-parallel β-strands wrapped around a central five-turn α-helix. There is considerable similarity between the structural features of free stefin A in solution and the X-ray structure of the homologous protein stefin B in its complex with papain, but there are also some important differences in the regions which are fundamental to proteinase binding. The differences consist primarily of two regions of high conformational heterogeneity in free stefin A which correspond in stefin B to two of the components of the tripartite wedge that docks into the active site of the target proteinase. These regions, which are shown to be mobile in solution, are the five N-terminal residues and the second binding loop. In the bound conformation of stefin B they form a turn and a short helix, respectively.</div>
</front>
</TEI>
<affiliations><list><country><li>Royaume-Uni</li>
<li>Slovénie</li>
</country>
</list>
<tree><country name="Royaume-Uni"><noRegion><name sortKey="Martin, John R" sort="Martin, John R" uniqKey="Martin J" first="John R." last="Martin">John R. Martin</name>
</noRegion>
<name sortKey="Craven, Jeremy C" sort="Craven, Jeremy C" uniqKey="Craven J" first="Jeremy C." last="Craven">Jeremy C. Craven</name>
<name sortKey="Waltho, Jonathan P" sort="Waltho, Jonathan P" uniqKey="Waltho J" first="Jonathan P." last="Waltho">Jonathan P. Waltho</name>
</country>
<country name="Slovénie"><noRegion><name sortKey="Jerala, Roman" sort="Jerala, Roman" uniqKey="Jerala R" first="Roman" last="Jerala">Roman Jerala</name>
</noRegion>
<name sortKey="Kroon Itko, Louise" sort="Kroon Itko, Louise" uniqKey="Kroon Itko L" first="Louise" last="Kroon-Žitko">Louise Kroon-Žitko</name>
<name sortKey="Turk, Vito" sort="Turk, Vito" uniqKey="Turk V" first="Vito" last="Turk">Vito Turk</name>
<name sortKey="Zerovnik, Eva" sort="Zerovnik, Eva" uniqKey="Zerovnik E" first="Eva" last="Žerovnik">Eva Žerovnik</name>
</country>
</tree>
</affiliations>
</record>

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Wicri/Informatique/explor/SgmlV1/Data/Main/Exploration

HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002D58 | SxmlIndent | more

HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 002D58 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Wicri/Informatique
   |area=    SgmlV1
   |flux=    Main
   |étape=   Exploration
   |type=    RBID
   |clé=     ISTEX:B067B0F1FAAA2AA83A2DF15AB7F12D1AC76B84C7
   |texte=   The Three-dimensional Solution Structure of Human Stefin A
}}

This area was generated with Dilib version V0.6.33.
Data generation: Mon Jul 1 14:26:08 2019. Site generation: Wed Apr 28 21:40:44 2021

	Serveur d'exploration sur SGML
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.

Serveur d'exploration sur SGML

The Three-dimensional Solution Structure of Human Stefin A

The Three-dimensional Solution Structure of Human Stefin A

Source :

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri