Mechanisms of Selectivity in Channels and Enzymes Studied with Interactive Molecular Dynamics
Identifieur interne : 000391 ( Ncbi/Merge ); précédent : 000390; suivant : 000392Mechanisms of Selectivity in Channels and Enzymes Studied with Interactive Molecular Dynamics
Auteurs : Paul Grayson ; Emad Tajkhorshid ; Klaus SchultenSource :
- Biophysical Journal [ 0006-3495 ] ; 2003.
Abstract
Interactive molecular dynamics, a new modeling tool for rapid investigation of the physical mechanisms of biological processes at the atomic level, is applied to study selectivity and regulation of the membrane channel protein GlpF and the enzyme glycerol kinase. These proteins facilitate the first two steps of
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PubMed: 12829462
PubMed Central: 1303063
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Mechanisms of Selectivity in Channels and Enzymes Studied with Interactive Molecular Dynamics</title><author><name sortKey="Grayson, Paul" sort="Grayson, Paul" uniqKey="Grayson P" first="Paul" last="Grayson">Paul Grayson</name></author><author><name sortKey="Tajkhorshid, Emad" sort="Tajkhorshid, Emad" uniqKey="Tajkhorshid E" first="Emad" last="Tajkhorshid">Emad Tajkhorshid</name></author><author><name sortKey="Schulten, Klaus" sort="Schulten, Klaus" uniqKey="Schulten K" first="Klaus" last="Schulten">Klaus Schulten</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">12829462</idno><idno type="pmc">1303063</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1303063</idno><idno type="RBID">PMC:1303063</idno><date when="2003">2003</date><idno type="wicri:Area/Pmc/Corpus">000982</idno><idno type="wicri:Area/Pmc/Curation">000982</idno><idno type="wicri:Area/Pmc/Checkpoint">002628</idno><idno type="wicri:Area/Ncbi/Merge">000391</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Mechanisms of Selectivity in Channels and Enzymes Studied with Interactive Molecular Dynamics</title><author><name sortKey="Grayson, Paul" sort="Grayson, Paul" uniqKey="Grayson P" first="Paul" last="Grayson">Paul Grayson</name></author><author><name sortKey="Tajkhorshid, Emad" sort="Tajkhorshid, Emad" uniqKey="Tajkhorshid E" first="Emad" last="Tajkhorshid">Emad Tajkhorshid</name></author><author><name sortKey="Schulten, Klaus" sort="Schulten, Klaus" uniqKey="Schulten K" first="Klaus" last="Schulten">Klaus Schulten</name></author></analytic><series><title level="j">Biophysical Journal</title><idno type="ISSN">0006-3495</idno><idno type="eISSN">1542-0086</idno><imprint><date when="2003">2003</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Interactive molecular dynamics, a new modeling tool for rapid investigation of the physical mechanisms of biological processes at the atomic level, is applied to study selectivity and regulation of the membrane channel protein GlpF and the enzyme glycerol kinase. These proteins facilitate the first two steps of <italic>Escherichia coli</italic> glycerol metabolism. Despite their different function and architecture the proteins are found to employ common mechanisms for substrate selectivity: an induced geometrical fit by structurally homologous binding sites and an induced rapid dipole moment reversal. Competition for hydrogen bonding sites with water in both proteins is critical for substrate motion. In glycerol kinase, it is shown that the proposed domain motion prevents competition with water, in turn regulating the binding of glycerol.</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">Biophys J</journal-id><journal-id journal-id-type="publisher-id">biophysj</journal-id><journal-title>Biophysical Journal</journal-title><issn pub-type="ppub">0006-3495</issn><issn pub-type="epub">1542-0086</issn><publisher><publisher-name>Biophysical Society</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">12829462</article-id><article-id pub-id-type="pmc">1303063</article-id><article-id pub-id-type="publisher-id">19935</article-id><article-categories><subj-group subj-group-type="heading"><subject>Biophysical Theory and Modeling</subject></subj-group></article-categories><title-group><article-title>Mechanisms of Selectivity in Channels and Enzymes Studied with Interactive Molecular Dynamics</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Grayson</surname><given-names>Paul</given-names></name></contrib><contrib contrib-type="author"><name><surname>Tajkhorshid</surname><given-names>Emad</given-names></name></contrib><contrib contrib-type="author"><name><surname>Schulten</surname><given-names>Klaus</given-names></name></contrib></contrib-group><aff id="N0x967c648.0x9ad0030">Beckman Institute, University of Illinois at Urbana-Champaign, Urbana, Illinois</aff><author-notes><fn><p>Address reprint requests to Klaus Schulten, <email>kschulte@ks.uiuc.edu</email>.</p></fn></author-notes><pub-date pub-type="ppub"><month>7</month><year>2003</year></pub-date><volume>85</volume><issue>1</issue><fpage>36</fpage><lpage>48</lpage><history><date date-type="received"><day>15</day><month>11</month><year>2002</year></date><date date-type="accepted"><day>25</day><month>2</month><year>2003</year></date></history><copyright-statement>Copyright © 2003, Biophysical Society</copyright-statement><copyright-year>2003</copyright-year><abstract><p>Interactive molecular dynamics, a new modeling tool for rapid investigation of the physical mechanisms of biological processes at the atomic level, is applied to study selectivity and regulation of the membrane channel protein GlpF and the enzyme glycerol kinase. These proteins facilitate the first two steps of <italic>Escherichia coli</italic> glycerol metabolism. Despite their different function and architecture the proteins are found to employ common mechanisms for substrate selectivity: an induced geometrical fit by structurally homologous binding sites and an induced rapid dipole moment reversal. Competition for hydrogen bonding sites with water in both proteins is critical for substrate motion. In glycerol kinase, it is shown that the proposed domain motion prevents competition with water, in turn regulating the binding of glycerol.</p></abstract></article-meta></front></pmc><affiliations><list></list><tree><noCountry><name sortKey="Grayson, Paul" sort="Grayson, Paul" uniqKey="Grayson P" first="Paul" last="Grayson">Paul Grayson</name><name sortKey="Schulten, Klaus" sort="Schulten, Klaus" uniqKey="Schulten K" first="Klaus" last="Schulten">Klaus Schulten</name><name sortKey="Tajkhorshid, Emad" sort="Tajkhorshid, Emad" uniqKey="Tajkhorshid E" first="Emad" last="Tajkhorshid">Emad Tajkhorshid</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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