Serpins Flex Their Muscle
Identifieur interne : 002474 ( Pmc/Checkpoint ); précédent : 002473; suivant : 002475Serpins Flex Their Muscle
Auteurs : James C. Whisstock ; Gary A. Silverman ; Phillip I. Bird ; Stephen P. Bottomley ; Dion Kaiserman ; Cliff J. Luke ; Stephen C. Pak ; Jean-Marc Reichhart ; James A. HuntingtonSource :
- The Journal of Biological Chemistry [ 0021-9258 ] ; 2010.
Abstract
Inhibitory serpins are metastable proteins that undergo a substantial conformational rearrangement to covalently trap target peptidases. The serpin reactive center loop contributes a majority of the interactions that serpins make during the initial binding to target peptidases. However, structural studies on serpin-peptidase complexes reveal a broader set of contacts on the scaffold of inhibitory serpins that have substantial influence on guiding peptidase recognition. Structural and biophysical studies also reveal how aberrant serpin folding can lead to the formation of domain-swapped serpin multimers rather than the monomeric metastable state. Serpin domain swapping may therefore underlie the polymerization events characteristic of the serpinopathies. Finally, recent structural studies reveal how the serpin fold has been adapted for non-inhibitory functions such as hormone binding.
Url:
DOI: 10.1074/jbc.R110.141408
PubMed: 20498368
PubMed Central: 2915666
Affiliations:
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Bottomley</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Kaiserman, Dion" sort="Kaiserman, Dion" uniqKey="Kaiserman D" first="Dion" last="Kaiserman">Dion Kaiserman</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Luke, Cliff J" sort="Luke, Cliff J" uniqKey="Luke C" first="Cliff J." last="Luke">Cliff J. Luke</name><affiliation><nlm:aff id="aff2"></nlm:aff></affiliation></author><author><name sortKey="Pak, Stephen C" sort="Pak, Stephen C" uniqKey="Pak S" first="Stephen C." last="Pak">Stephen C. Pak</name><affiliation><nlm:aff id="aff2"></nlm:aff></affiliation></author><author><name sortKey="Reichhart, Jean Marc" sort="Reichhart, Jean Marc" uniqKey="Reichhart J" first="Jean-Marc" last="Reichhart">Jean-Marc Reichhart</name><affiliation><nlm:aff id="aff3"></nlm:aff></affiliation></author><author><name sortKey="Huntington, James A" sort="Huntington, James A" uniqKey="Huntington J" first="James A." last="Huntington">James A. Huntington</name><affiliation><nlm:aff id="aff4"></nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">20498368</idno><idno type="pmc">2915666</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2915666</idno><idno type="RBID">PMC:2915666</idno><idno type="doi">10.1074/jbc.R110.141408</idno><date when="2010">2010</date><idno type="wicri:Area/Pmc/Corpus">002E85</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">002E85</idno><idno type="wicri:Area/Pmc/Curation">002D34</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">002D34</idno><idno type="wicri:Area/Pmc/Checkpoint">002474</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">002474</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Serpins Flex Their Muscle</title><author><name sortKey="Whisstock, James C" sort="Whisstock, James C" uniqKey="Whisstock J" first="James C." last="Whisstock">James C. Whisstock</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Silverman, Gary A" sort="Silverman, Gary A" uniqKey="Silverman G" first="Gary A." last="Silverman">Gary A. Silverman</name><affiliation><nlm:aff id="aff2"></nlm:aff></affiliation></author><author><name sortKey="Bird, Phillip I" sort="Bird, Phillip I" uniqKey="Bird P" first="Phillip I." last="Bird">Phillip I. Bird</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Bottomley, Stephen P" sort="Bottomley, Stephen P" uniqKey="Bottomley S" first="Stephen P." last="Bottomley">Stephen P. Bottomley</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Kaiserman, Dion" sort="Kaiserman, Dion" uniqKey="Kaiserman D" first="Dion" last="Kaiserman">Dion Kaiserman</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Luke, Cliff J" sort="Luke, Cliff J" uniqKey="Luke C" first="Cliff J." last="Luke">Cliff J. Luke</name><affiliation><nlm:aff id="aff2"></nlm:aff></affiliation></author><author><name sortKey="Pak, Stephen C" sort="Pak, Stephen C" uniqKey="Pak S" first="Stephen C." last="Pak">Stephen C. Pak</name><affiliation><nlm:aff id="aff2"></nlm:aff></affiliation></author><author><name sortKey="Reichhart, Jean Marc" sort="Reichhart, Jean Marc" uniqKey="Reichhart J" first="Jean-Marc" last="Reichhart">Jean-Marc Reichhart</name><affiliation><nlm:aff id="aff3"></nlm:aff></affiliation></author><author><name sortKey="Huntington, James A" sort="Huntington, James A" uniqKey="Huntington J" first="James A." last="Huntington">James A. Huntington</name><affiliation><nlm:aff id="aff4"></nlm:aff></affiliation></author></analytic><series><title level="j">The Journal of Biological Chemistry</title><idno type="ISSN">0021-9258</idno><idno type="eISSN">1083-351X</idno><imprint><date when="2010">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Inhibitory serpins are metastable proteins that undergo a substantial conformational rearrangement to covalently trap target peptidases. The serpin reactive center loop contributes a majority of the interactions that serpins make during the initial binding to target peptidases. However, structural studies on serpin-peptidase complexes reveal a broader set of contacts on the scaffold of inhibitory serpins that have substantial influence on guiding peptidase recognition. Structural and biophysical studies also reveal how aberrant serpin folding can lead to the formation of domain-swapped serpin multimers rather than the monomeric metastable state. Serpin domain swapping may therefore underlie the polymerization events characteristic of the serpinopathies. Finally, recent structural studies reveal how the serpin fold has been adapted for non-inhibitory functions such as hormone binding.</p></div></front></TEI><pmc article-type="review-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">J Biol Chem</journal-id><journal-id journal-id-type="hwp">jbc</journal-id><journal-id journal-id-type="pmc">jbc</journal-id><journal-id journal-id-type="publisher-id">JBC</journal-id><journal-title-group><journal-title>The Journal of Biological Chemistry</journal-title></journal-title-group><issn pub-type="ppub">0021-9258</issn><issn pub-type="epub">1083-351X</issn><publisher><publisher-name>American Society for Biochemistry and Molecular Biology</publisher-name><publisher-loc>9650 Rockville Pike, Bethesda, MD 20814, U.S.A.</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">20498368</article-id><article-id pub-id-type="pmc">2915666</article-id><article-id pub-id-type="publisher-id">R110.141408</article-id><article-id pub-id-type="doi">10.1074/jbc.R110.141408</article-id><article-categories><subj-group subj-group-type="heading"><subject>Minireviews</subject></subj-group><subj-group><subject>Cell Biology</subject></subj-group></article-categories><title-group><article-title>Serpins Flex Their Muscle</article-title><subtitle>II. STRUCTURAL INSIGHTS INTO TARGET PEPTIDASE RECOGNITION, POLYMERIZATION, AND TRANSPORT FUNCTIONS<xref ref-type="fn" rid="FN1">*</xref></subtitle><alt-title alt-title-type="short">MINIREVIEW: Serpin Structural Insights</alt-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Whisstock</surname><given-names>James C.</given-names></name><xref ref-type="aff" rid="aff1"><sup>‡</sup></xref><xref ref-type="corresp" rid="cor1"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Silverman</surname><given-names>Gary A.</given-names></name><xref ref-type="aff" rid="aff2"><sup>§</sup></xref><xref ref-type="corresp" rid="cor2"><sup>2</sup></xref></contrib><contrib contrib-type="author"><name><surname>Bird</surname><given-names>Phillip I.</given-names></name><xref ref-type="aff" rid="aff1"><sup>‡</sup></xref></contrib><contrib contrib-type="author"><name><surname>Bottomley</surname><given-names>Stephen P.</given-names></name><xref ref-type="aff" rid="aff1"><sup>‡</sup></xref></contrib><contrib contrib-type="author"><name><surname>Kaiserman</surname><given-names>Dion</given-names></name><xref ref-type="aff" rid="aff1"><sup>‡</sup></xref></contrib><contrib contrib-type="author"><name><surname>Luke</surname><given-names>Cliff J.</given-names></name><xref ref-type="aff" rid="aff2"><sup>§</sup></xref></contrib><contrib contrib-type="author"><name><surname>Pak</surname><given-names>Stephen C.</given-names></name><xref ref-type="aff" rid="aff2"><sup>§</sup></xref></contrib><contrib contrib-type="author"><name><surname>Reichhart</surname><given-names>Jean-Marc</given-names></name><xref ref-type="aff" rid="aff3"><sup>¶</sup></xref></contrib><contrib contrib-type="author"><name><surname>Huntington</surname><given-names>James A.</given-names></name><xref ref-type="aff" rid="aff4"><sup>‖</sup></xref></contrib><aff id="aff1">From the<label>‡</label>Department of Biochemistry and Molecular Biology and ARC Centre of Excellence in Structural and Functional Microbial Genomics, Monash University, Clayton, Victoria 3800, Australia,</aff><aff id="aff2">the<label>§</label>Departments of Pediatrics and Cell Biology and Physiology, Children's Hospital of Pittsburgh and Magee-Womens Hospital, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15201,</aff><aff id="aff3">the<label>¶</label>Université de Strasbourg, CNRS UPR 9022, Institut de Biologie Moléculaire et Cellulaire, 67084 Strasbourg Cedex, France, and</aff><aff id="aff4">the<label>‖</label>Department of Haematology, Cambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 0XY, United Kingdom</aff></contrib-group><author-notes><corresp id="cor1"><label>1</label> Australian Research Council Federation Fellow and Honorary National Health and Medical Research Council Australia Principal Research Fellow. To whom correspondence may be addressed. E-mail: <email>james.whisstock@monash.edu.au</email>.</corresp><corresp id="cor2"><label>2</label> To whom correspondence may be addressed. E-mail: <email>gsilverman@upmc.edu</email>.</corresp></author-notes><pub-date pub-type="ppub"><day>6</day><month>8</month><year>2010</year></pub-date><pub-date pub-type="epub"><day>24</day><month>5</month><year>2010</year></pub-date><volume>285</volume><issue>32</issue><fpage>24307</fpage><lpage>24312</lpage><permissions><copyright-statement>© 2010 by The American Society for Biochemistry and Molecular Biology, Inc.</copyright-statement></permissions><self-uri xlink:title="pdf" xlink:type="simple" xlink:href="zbc03210024307.pdf"></self-uri><abstract><p>Inhibitory serpins are metastable proteins that undergo a substantial conformational rearrangement to covalently trap target peptidases. The serpin reactive center loop contributes a majority of the interactions that serpins make during the initial binding to target peptidases. However, structural studies on serpin-peptidase complexes reveal a broader set of contacts on the scaffold of inhibitory serpins that have substantial influence on guiding peptidase recognition. Structural and biophysical studies also reveal how aberrant serpin folding can lead to the formation of domain-swapped serpin multimers rather than the monomeric metastable state. Serpin domain swapping may therefore underlie the polymerization events characteristic of the serpinopathies. Finally, recent structural studies reveal how the serpin fold has been adapted for non-inhibitory functions such as hormone binding.</p></abstract><kwd-group><kwd>Antithrombin</kwd><kwd>Crystal Structure</kwd><kwd>Peptidases</kwd><kwd>Plasmin</kwd><kwd>Protease Inhibitor</kwd><kwd>Protein Domains</kwd><kwd>Protein Structure</kwd><kwd>Serine Protease</kwd><kwd>Serpin</kwd><kwd>Thrombin</kwd></kwd-group><funding-group><award-group><funding-source id="CS100">National Institutes of Health</funding-source><award-id rid="CS100">DK079806</award-id><award-id rid="CS100">DK081422</award-id><award-id rid="CS100">HL68629</award-id></award-group></funding-group></article-meta></front></pmc><affiliations><list></list><tree><noCountry><name sortKey="Bird, Phillip I" sort="Bird, Phillip I" uniqKey="Bird P" first="Phillip I." last="Bird">Phillip I. Bird</name><name sortKey="Bottomley, Stephen P" sort="Bottomley, Stephen P" uniqKey="Bottomley S" first="Stephen P." last="Bottomley">Stephen P. Bottomley</name><name sortKey="Huntington, James A" sort="Huntington, James A" uniqKey="Huntington J" first="James A." last="Huntington">James A. Huntington</name><name sortKey="Kaiserman, Dion" sort="Kaiserman, Dion" uniqKey="Kaiserman D" first="Dion" last="Kaiserman">Dion Kaiserman</name><name sortKey="Luke, Cliff J" sort="Luke, Cliff J" uniqKey="Luke C" first="Cliff J." last="Luke">Cliff J. Luke</name><name sortKey="Pak, Stephen C" sort="Pak, Stephen C" uniqKey="Pak S" first="Stephen C." last="Pak">Stephen C. Pak</name><name sortKey="Reichhart, Jean Marc" sort="Reichhart, Jean Marc" uniqKey="Reichhart J" first="Jean-Marc" last="Reichhart">Jean-Marc Reichhart</name><name sortKey="Silverman, Gary A" sort="Silverman, Gary A" uniqKey="Silverman G" first="Gary A." last="Silverman">Gary A. Silverman</name><name sortKey="Whisstock, James C" sort="Whisstock, James C" uniqKey="Whisstock J" first="James C." last="Whisstock">James C. 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