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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Experimentally exploring the conformational space sampled by domain reorientation in calmodulin</title><author><name sortKey="Bertini, Ivano" sort="Bertini, Ivano" uniqKey="Bertini I" first="Ivano" last="Bertini">Ivano Bertini</name><affiliation><nlm:aff id="N0x9cc9d88.0x9812840">Centre for Magnetic Resonance and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, I-50019 Sesto Fiorentino, Italy;</nlm:aff></affiliation></author><author><name sortKey="Del Bianco, Cristina" sort="Del Bianco, Cristina" uniqKey="Del Bianco C" first="Cristina" last="Del Bianco">Cristina Del Bianco</name><affiliation><nlm:aff id="N0x9cc9d88.0x9812840">Centre for Magnetic Resonance and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, I-50019 Sesto Fiorentino, Italy;</nlm:aff></affiliation></author><author><name sortKey="Gelis, Ioannis" sort="Gelis, Ioannis" uniqKey="Gelis I" first="Ioannis" last="Gelis">Ioannis Gelis</name><affiliation><nlm:aff id="N0x9cc9d88.0x9812840">National Centre for Scientific Research Demokritos, Institute of Physical Chemistry, 15310 Agia Paraskevi Attikis, Greece;</nlm:aff></affiliation></author><author><name sortKey="Katsaros, Nikolaus" sort="Katsaros, Nikolaus" uniqKey="Katsaros N" first="Nikolaus" last="Katsaros">Nikolaus Katsaros</name><affiliation><nlm:aff id="N0x9cc9d88.0x9812840">National Centre for Scientific Research Demokritos, Institute of Physical Chemistry, 15310 Agia Paraskevi Attikis, Greece;</nlm:aff></affiliation></author><author><name sortKey="Luchinat, Claudio" sort="Luchinat, Claudio" uniqKey="Luchinat C" first="Claudio" last="Luchinat">Claudio Luchinat</name><affiliation><nlm:aff wicri:cut="; and" id="N0x9cc9d88.0x9812840">Centre for Magnetic Resonance and Department of Agricultural Biotechnology, University of Florence, Piazzale delle Cascine 28, I-50144 Florence, Italy</nlm:aff></affiliation></author><author><name sortKey="Parigi, Giacomo" sort="Parigi, Giacomo" uniqKey="Parigi G" first="Giacomo" last="Parigi">Giacomo Parigi</name><affiliation><nlm:aff wicri:cut="; and" id="N0x9cc9d88.0x9812840">Centre for Magnetic Resonance and Department of Agricultural Biotechnology, University of Florence, Piazzale delle Cascine 28, I-50144 Florence, Italy</nlm:aff></affiliation></author><author><name sortKey="Peana, Massimiliano" sort="Peana, Massimiliano" uniqKey="Peana M" first="Massimiliano" last="Peana">Massimiliano Peana</name><affiliation><nlm:aff id="N0x9cc9d88.0x9812840">Department of Chemistry, University of Sassari, Via Vienna 2, 07100 Sassari, Italy</nlm:aff></affiliation></author><author><name sortKey="Provenzani, Alessandro" sort="Provenzani, Alessandro" uniqKey="Provenzani A" first="Alessandro" last="Provenzani">Alessandro Provenzani</name><affiliation><nlm:aff id="N0x9cc9d88.0x9812840">Centre for Magnetic Resonance and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, I-50019 Sesto Fiorentino, Italy;</nlm:aff></affiliation></author><author><name sortKey="Zoroddu, Maria Antonietta" sort="Zoroddu, Maria Antonietta" uniqKey="Zoroddu M" first="Maria Antonietta" last="Zoroddu">Maria Antonietta Zoroddu</name><affiliation><nlm:aff id="N0x9cc9d88.0x9812840">Department of Chemistry, University of Sassari, Via Vienna 2, 07100 Sassari, Italy</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">15100408</idno><idno type="pmc">406429</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC406429</idno><idno type="RBID">PMC:406429</idno><idno type="doi">10.1073/pnas.0308641101</idno><date when="2004">2004</date><idno type="wicri:Area/Pmc/Corpus">000179</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000179</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Experimentally exploring the conformational space sampled by domain reorientation in calmodulin</title><author><name sortKey="Bertini, Ivano" sort="Bertini, Ivano" uniqKey="Bertini I" first="Ivano" last="Bertini">Ivano Bertini</name><affiliation><nlm:aff id="N0x9cc9d88.0x9812840">Centre for Magnetic Resonance and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, I-50019 Sesto Fiorentino, Italy;</nlm:aff></affiliation></author><author><name sortKey="Del Bianco, Cristina" sort="Del Bianco, Cristina" uniqKey="Del Bianco C" first="Cristina" last="Del Bianco">Cristina Del Bianco</name><affiliation><nlm:aff id="N0x9cc9d88.0x9812840">Centre for Magnetic Resonance and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, I-50019 Sesto Fiorentino, Italy;</nlm:aff></affiliation></author><author><name sortKey="Gelis, Ioannis" sort="Gelis, Ioannis" uniqKey="Gelis I" first="Ioannis" last="Gelis">Ioannis Gelis</name><affiliation><nlm:aff id="N0x9cc9d88.0x9812840">National Centre for Scientific Research Demokritos, Institute of Physical Chemistry, 15310 Agia Paraskevi Attikis, Greece;</nlm:aff></affiliation></author><author><name sortKey="Katsaros, Nikolaus" sort="Katsaros, Nikolaus" uniqKey="Katsaros N" first="Nikolaus" last="Katsaros">Nikolaus Katsaros</name><affiliation><nlm:aff id="N0x9cc9d88.0x9812840">National Centre for Scientific Research Demokritos, Institute of Physical Chemistry, 15310 Agia Paraskevi Attikis, Greece;</nlm:aff></affiliation></author><author><name sortKey="Luchinat, Claudio" sort="Luchinat, Claudio" uniqKey="Luchinat C" first="Claudio" last="Luchinat">Claudio Luchinat</name><affiliation><nlm:aff wicri:cut="; and" id="N0x9cc9d88.0x9812840">Centre for Magnetic Resonance and Department of Agricultural Biotechnology, University of Florence, Piazzale delle Cascine 28, I-50144 Florence, Italy</nlm:aff></affiliation></author><author><name sortKey="Parigi, Giacomo" sort="Parigi, Giacomo" uniqKey="Parigi G" first="Giacomo" last="Parigi">Giacomo Parigi</name><affiliation><nlm:aff wicri:cut="; and" id="N0x9cc9d88.0x9812840">Centre for Magnetic Resonance and Department of Agricultural Biotechnology, University of Florence, Piazzale delle Cascine 28, I-50144 Florence, Italy</nlm:aff></affiliation></author><author><name sortKey="Peana, Massimiliano" sort="Peana, Massimiliano" uniqKey="Peana M" first="Massimiliano" last="Peana">Massimiliano Peana</name><affiliation><nlm:aff id="N0x9cc9d88.0x9812840">Department of Chemistry, University of Sassari, Via Vienna 2, 07100 Sassari, Italy</nlm:aff></affiliation></author><author><name sortKey="Provenzani, Alessandro" sort="Provenzani, Alessandro" uniqKey="Provenzani A" first="Alessandro" last="Provenzani">Alessandro Provenzani</name><affiliation><nlm:aff id="N0x9cc9d88.0x9812840">Centre for Magnetic Resonance and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, I-50019 Sesto Fiorentino, Italy;</nlm:aff></affiliation></author><author><name sortKey="Zoroddu, Maria Antonietta" sort="Zoroddu, Maria Antonietta" uniqKey="Zoroddu M" first="Maria Antonietta" last="Zoroddu">Maria Antonietta Zoroddu</name><affiliation><nlm:aff id="N0x9cc9d88.0x9812840">Department of Chemistry, University of Sassari, Via Vienna 2, 07100 Sassari, Italy</nlm:aff></affiliation></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="ISSN">0027-8424</idno><idno type="eISSN">1091-6490</idno><imprint><date when="2004">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>The conformational space sampled by the two-domain protein calmodulin has been explored by an approach based on four sets of NMR observables obtained on Tb<sup>3+</sup>- and Tm<sup>3+</sup>-substituted proteins. The observables are the pseudocontact shifts and residual dipolar couplings of the C-terminal domain when lanthanide substitution is at the N-terminal domain. Each set of observables provides independent information on the conformations experienced by the molecule. It is found that not all sterically allowed conformations are equally populated. Taking the N-terminal domain as the reference, the C-terminal domain preferentially resides in a region of space inscribed in a wide elliptical cone. The axis of the cone is tilted by ≈30° with respect to the direction of the N-terminal part of the interdomain helix, which is known to have a flexible central part in solution. The C-terminal domain also undergoes rotation about the axis defined by the C-terminal part of the interdomain helix. Neither the extended helix conformation initially observed in the solid state for free calcium calmodulin nor the closed conformation(s) adopted by calcium calmodulin either alone or in its adduct(s) with target peptide(s) is among the most preferred ones. These findings are unique, both in terms of structural information obtained on a biomolecule that samples multiple conformations and in terms of the approach developed to achieve the results. The same approach is in principle applicable to other multidomain proteins, as well as to multiple interaction modes between two macromolecular partners.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Proc Natl Acad Sci U S A</journal-id><journal-id journal-id-type="publisher-id">pnas</journal-id><journal-title>Proceedings of the National Academy of Sciences of the United States of America</journal-title><issn pub-type="ppub">0027-8424</issn><issn pub-type="epub">1091-6490</issn><publisher><publisher-name>National Academy of Sciences</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">15100408</article-id><article-id pub-id-type="pmc">406429</article-id><article-id pub-id-type="publisher-id">1016841</article-id><article-id pub-id-type="doi">10.1073/pnas.0308641101</article-id><article-categories><subj-group subj-group-type="heading"><subject>Physical Sciences</subject><subj-group><subject>Chemistry</subject></subj-group></subj-group><series-title>From the Cover</series-title></article-categories><title-group><article-title>Experimentally exploring the conformational space sampled by domain reorientation in calmodulin</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Bertini</surname><given-names>Ivano</given-names></name><xref ref-type="aff" rid="N0x9cc9d88.0x9812840">*</xref><xref ref-type="corresp" rid="cor1">†</xref></contrib><contrib contrib-type="author"><name><surname>Del Bianco</surname><given-names>Cristina</given-names></name><xref ref-type="aff" rid="N0x9cc9d88.0x9812840">*</xref></contrib><contrib contrib-type="author"><name><surname>Gelis</surname><given-names>Ioannis</given-names></name><xref ref-type="aff" rid="N0x9cc9d88.0x9812840">‡</xref></contrib><contrib contrib-type="author"><name><surname>Katsaros</surname><given-names>Nikolaus</given-names></name><xref ref-type="aff" rid="N0x9cc9d88.0x9812840">‡</xref></contrib><contrib contrib-type="author"><name><surname>Luchinat</surname><given-names>Claudio</given-names></name><xref ref-type="aff" rid="N0x9cc9d88.0x9812840">§</xref></contrib><contrib contrib-type="author"><name><surname>Parigi</surname><given-names>Giacomo</given-names></name><xref ref-type="aff" rid="N0x9cc9d88.0x9812840">§</xref></contrib><contrib contrib-type="author"><name><surname>Peana</surname><given-names>Massimiliano</given-names></name><xref ref-type="aff" rid="N0x9cc9d88.0x9812840">¶</xref></contrib><contrib contrib-type="author"><name><surname>Provenzani</surname><given-names>Alessandro</given-names></name><xref ref-type="aff" rid="N0x9cc9d88.0x9812840">*</xref></contrib><contrib contrib-type="author"><name><surname>Zoroddu</surname><given-names>Maria Antonietta</given-names></name><xref ref-type="aff" rid="N0x9cc9d88.0x9812840">¶</xref></contrib></contrib-group><aff id="N0x9cc9d88.0x9812840"><label>*</label>Centre for Magnetic Resonance and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, I-50019 Sesto Fiorentino, Italy;<label>‡</label>National Centre for Scientific Research Demokritos, Institute of Physical Chemistry, 15310 Agia Paraskevi Attikis, Greece;<label>§</label>Centre for Magnetic Resonance and Department of Agricultural Biotechnology, University of Florence, Piazzale delle Cascine 28, I-50144 Florence, Italy; and<label>¶</label>Department of Chemistry, University of Sassari, Via Vienna 2, 07100 Sassari, Italy</aff><author-notes><fn id="cor1"><label>†</label><p> To whom correspondence should be addressed at: Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino (FI), Italy. E-mail: <email>bertini@cerm.unifi.it</email>. </p></fn><fn><p>Edited by Harry B. Gray, California Institute of Technology, Pasadena, CA</p></fn></author-notes><pub-date pub-type="ppub"><day>4</day><month>5</month><year>2004</year></pub-date><pub-date pub-type="epub"><day>20</day><month>4</month><year>2004</year></pub-date><volume>101</volume><issue>18</issue><fpage>6841</fpage><lpage>6846</lpage><history><date date-type="received"><day>24</day><month>12</month><year>2003</year></date><date date-type="accepted"><day>5</day><month>3</month><year>2004</year></date></history><copyright-statement>Copyright © 2004, The National Academy of Sciences</copyright-statement><copyright-year>2004</copyright-year><abstract><p>The conformational space sampled by the two-domain protein calmodulin has been explored by an approach based on four sets of NMR observables obtained on Tb<sup>3+</sup>- and Tm<sup>3+</sup>-substituted proteins. The observables are the pseudocontact shifts and residual dipolar couplings of the C-terminal domain when lanthanide substitution is at the N-terminal domain. Each set of observables provides independent information on the conformations experienced by the molecule. It is found that not all sterically allowed conformations are equally populated. Taking the N-terminal domain as the reference, the C-terminal domain preferentially resides in a region of space inscribed in a wide elliptical cone. The axis of the cone is tilted by ≈30° with respect to the direction of the N-terminal part of the interdomain helix, which is known to have a flexible central part in solution. The C-terminal domain also undergoes rotation about the axis defined by the C-terminal part of the interdomain helix. Neither the extended helix conformation initially observed in the solid state for free calcium calmodulin nor the closed conformation(s) adopted by calcium calmodulin either alone or in its adduct(s) with target peptide(s) is among the most preferred ones. These findings are unique, both in terms of structural information obtained on a biomolecule that samples multiple conformations and in terms of the approach developed to achieve the results. The same approach is in principle applicable to other multidomain proteins, as well as to multiple interaction modes between two macromolecular partners.</p></abstract></article-meta><notes><fn-group><fn><p>This paper was submitted directly (Track II) to the PNAS office.</p></fn><fn><p>Abbreviations: CaM, calmodulin; pcs, pseudocontact shifts; rdc, residual dipolar couplings; Ln, lanthanide; HSQC, heteronuclear sequential quantum correlation; NOE, nuclear Overhauser enhancement.</p></fn><fn><p>Data deposition: The solution structures have been deposited in the Protein Data Bank, <ext-link ext-link-type="uri" xlink:href="www.pdb.org">www.pdb.org</ext-link> (PDB ID code 1SW8).</p></fn></fn-group></notes></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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