Crystal Structure of the Central Region of Bovine Fibrinogen (E5Fragment) at 1.4-Å Resolution
The high-resolution crystal structure of the N-terminal central region of bovine fibrinogen (a 35-kDa E5fragment) reveals a remarkable dimeric design. The two halves of the molecule bond together at the center in an extensive molecular "handshake" by using both disulfide linkages and nonco...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2001-10, Vol.98 (21), p.11967-11972 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Madrazo, Joel Brown, Jerry H. Litvinovich, Sergei Dominguez, Roberto Yakovlev, Sergei Medved, Leonid Cohen, Carolyn |
| description | The high-resolution crystal structure of the N-terminal central region of bovine fibrinogen (a 35-kDa E5fragment) reveals a remarkable dimeric design. The two halves of the molecule bond together at the center in an extensive molecular "handshake" by using both disulfide linkages and noncovalent contacts. On one face of the fragment, the Aα and Bβ chains from the two monomers form a funnel-shaped domain with an unusual hydrophobic cavity; here, on each of the two outer sides there appears to be a binding site for thrombin. On the opposite face, the N-terminal γ chains fold into a separate domain. Despite the chemical identity of the two halves of fibrinogen, an unusual pair of adjacent disulfide bonds locally constrain the two γ chains to adopt different conformations. The striking asymmetry of this domain may promote the known supercoiling of the protofibrils in fibrin. This information on the detailed topology of the E5fragment permits the construction of a more detailed model than previously possible for the critical trimolecular junction of the protofibril in fibrin. |
| doi_str_mv | 10.1073/pnas.211439798 |
| format | Article |
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The two halves of the molecule bond together at the center in an extensive molecular "handshake" by using both disulfide linkages and noncovalent contacts. On one face of the fragment, the Aα and Bβ chains from the two monomers form a funnel-shaped domain with an unusual hydrophobic cavity; here, on each of the two outer sides there appears to be a binding site for thrombin. On the opposite face, the N-terminal γ chains fold into a separate domain. Despite the chemical identity of the two halves of fibrinogen, an unusual pair of adjacent disulfide bonds locally constrain the two γ chains to adopt different conformations. The striking asymmetry of this domain may promote the known supercoiling of the protofibrils in fibrin. This information on the detailed topology of the E5fragment permits the construction of a more detailed model than previously possible for the critical trimolecular junction of the protofibril in fibrin.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.211439798</identifier><identifier>PMID: 11593005</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Amino Acid Sequence ; Animals ; Asymmetry ; Biological Sciences ; Cattle ; Chemical bonding ; Crystal structure ; Crystallography, X-Ray ; Dimerization ; Dimers ; Disulfides ; E layer ; Fibrin Fibrinogen Degradation Products - chemistry ; Fibrinogen - chemistry ; Models, Molecular ; Molecular chains ; Molecular Sequence Data ; Molecular structure ; Molecules ; Protein Structure, Tertiary ; Ungulates</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2001-10, Vol.98 (21), p.11967-11972</ispartof><rights>Copyright 1993-2001 National Academy of Sciences of the United States of America</rights><rights>Copyright © 2001, The National Academy of Sciences 2001</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4438-6103b58e3c2b029a928d7c26de1d2de9efde73cc6db556a3f4288b638ff0cb23</citedby><cites>FETCH-LOGICAL-c4438-6103b58e3c2b029a928d7c26de1d2de9efde73cc6db556a3f4288b638ff0cb23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/98/21.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3056832$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3056832$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11593005$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Madrazo, Joel</creatorcontrib><creatorcontrib>Brown, Jerry H.</creatorcontrib><creatorcontrib>Litvinovich, Sergei</creatorcontrib><creatorcontrib>Dominguez, Roberto</creatorcontrib><creatorcontrib>Yakovlev, Sergei</creatorcontrib><creatorcontrib>Medved, Leonid</creatorcontrib><creatorcontrib>Cohen, Carolyn</creatorcontrib><title>Crystal Structure of the Central Region of Bovine Fibrinogen (E5Fragment) at 1.4-Å Resolution</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The high-resolution crystal structure of the N-terminal central region of bovine fibrinogen (a 35-kDa E5fragment) reveals a remarkable dimeric design. The two halves of the molecule bond together at the center in an extensive molecular "handshake" by using both disulfide linkages and noncovalent contacts. On one face of the fragment, the Aα and Bβ chains from the two monomers form a funnel-shaped domain with an unusual hydrophobic cavity; here, on each of the two outer sides there appears to be a binding site for thrombin. On the opposite face, the N-terminal γ chains fold into a separate domain. Despite the chemical identity of the two halves of fibrinogen, an unusual pair of adjacent disulfide bonds locally constrain the two γ chains to adopt different conformations. The striking asymmetry of this domain may promote the known supercoiling of the protofibrils in fibrin. This information on the detailed topology of the E5fragment permits the construction of a more detailed model than previously possible for the critical trimolecular junction of the protofibril in fibrin.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Asymmetry</subject><subject>Biological Sciences</subject><subject>Cattle</subject><subject>Chemical bonding</subject><subject>Crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>Dimerization</subject><subject>Dimers</subject><subject>Disulfides</subject><subject>E layer</subject><subject>Fibrin Fibrinogen Degradation Products - chemistry</subject><subject>Fibrinogen - chemistry</subject><subject>Models, Molecular</subject><subject>Molecular chains</subject><subject>Molecular Sequence Data</subject><subject>Molecular structure</subject><subject>Molecules</subject><subject>Protein Structure, Tertiary</subject><subject>Ungulates</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kc1uEzEURi0EoiGwZYVgVqgsJlz_zdgSmxI1BakSEnSN5fHcSaeajIPtqdoH4Ml4MRwlDbBhZcnfOddX_gh5SWFBoebvt6ONC0ap4LrW6hGZUdC0rISGx2QGwOpSCSZOyLMYbwBASwVPyQmlUnMAOSPfl-E-JjsU31KYXJoCFr4r0jUWSxxTyMFXXPd-3N1-9Lf9iMWqb0I_-jWOxem5XAW73mT0XWFTQRei_PUzK9EPU8rac_Kks0PEF4dzTq5W51fLT-Xll4vPy7PL0gnBVVlR4I1UyB1rgGmrmWprx6oWacta1Ni1WHPnqraRsrK8E0yppuKq68A1jM_Jh_3Y7dRssHX71c029Bsb7o23vfk3Gftrs_a3Rupa0qy_PejB_5gwJrPpo8NhsCP6KZqaUSVU_rI5WexBF3yMAbvjExTMrg-z68Mc-8jC678X-4MfCsjA6QHYiQ-xVnlGhnRVm24ahoR3KaNv_o9m4tWeuInJhyPCQVaKM_4b8laptw</recordid><startdate>20011009</startdate><enddate>20011009</enddate><creator>Madrazo, Joel</creator><creator>Brown, Jerry H.</creator><creator>Litvinovich, Sergei</creator><creator>Dominguez, Roberto</creator><creator>Yakovlev, Sergei</creator><creator>Medved, Leonid</creator><creator>Cohen, Carolyn</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><general>The National Academy of Sciences</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20011009</creationdate><title>Crystal Structure of the Central Region of Bovine Fibrinogen (E5Fragment) at 1.4-Å Resolution</title><author>Madrazo, Joel ; Brown, Jerry H. ; Litvinovich, Sergei ; Dominguez, Roberto ; Yakovlev, Sergei ; Medved, Leonid ; Cohen, Carolyn</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4438-6103b58e3c2b029a928d7c26de1d2de9efde73cc6db556a3f4288b638ff0cb23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Asymmetry</topic><topic>Biological Sciences</topic><topic>Cattle</topic><topic>Chemical bonding</topic><topic>Crystal structure</topic><topic>Crystallography, X-Ray</topic><topic>Dimerization</topic><topic>Dimers</topic><topic>Disulfides</topic><topic>E layer</topic><topic>Fibrin Fibrinogen Degradation Products - chemistry</topic><topic>Fibrinogen - chemistry</topic><topic>Models, Molecular</topic><topic>Molecular chains</topic><topic>Molecular Sequence Data</topic><topic>Molecular structure</topic><topic>Molecules</topic><topic>Protein Structure, Tertiary</topic><topic>Ungulates</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Madrazo, Joel</creatorcontrib><creatorcontrib>Brown, Jerry H.</creatorcontrib><creatorcontrib>Litvinovich, Sergei</creatorcontrib><creatorcontrib>Dominguez, Roberto</creatorcontrib><creatorcontrib>Yakovlev, Sergei</creatorcontrib><creatorcontrib>Medved, Leonid</creatorcontrib><creatorcontrib>Cohen, Carolyn</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Madrazo, Joel</au><au>Brown, Jerry H.</au><au>Litvinovich, Sergei</au><au>Dominguez, Roberto</au><au>Yakovlev, Sergei</au><au>Medved, Leonid</au><au>Cohen, Carolyn</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal Structure of the Central Region of Bovine Fibrinogen (E5Fragment) at 1.4-Å Resolution</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2001-10-09</date><risdate>2001</risdate><volume>98</volume><issue>21</issue><spage>11967</spage><epage>11972</epage><pages>11967-11972</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>The high-resolution crystal structure of the N-terminal central region of bovine fibrinogen (a 35-kDa E5fragment) reveals a remarkable dimeric design. The two halves of the molecule bond together at the center in an extensive molecular "handshake" by using both disulfide linkages and noncovalent contacts. On one face of the fragment, the Aα and Bβ chains from the two monomers form a funnel-shaped domain with an unusual hydrophobic cavity; here, on each of the two outer sides there appears to be a binding site for thrombin. On the opposite face, the N-terminal γ chains fold into a separate domain. Despite the chemical identity of the two halves of fibrinogen, an unusual pair of adjacent disulfide bonds locally constrain the two γ chains to adopt different conformations. The striking asymmetry of this domain may promote the known supercoiling of the protofibrils in fibrin. This information on the detailed topology of the E5fragment permits the construction of a more detailed model than previously possible for the critical trimolecular junction of the protofibril in fibrin.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>11593005</pmid><doi>10.1073/pnas.211439798</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Animals Asymmetry Biological Sciences Cattle Chemical bonding Crystal structure Crystallography, X-Ray Dimerization Dimers Disulfides E layer Fibrin Fibrinogen Degradation Products - chemistry Fibrinogen - chemistry Models, Molecular Molecular chains Molecular Sequence Data Molecular structure Molecules Protein Structure, Tertiary Ungulates |
| title | Crystal Structure of the Central Region of Bovine Fibrinogen (E5Fragment) at 1.4-Å Resolution |
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