1m11

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Current revision (07:38, 14 February 2024) (edit) (undo)
 
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<SX load='1m11' size='340' side='right' viewer='molstar' caption='[[1m11]], [[Resolution|resolution]] 16.00&Aring;' scene=''>
<SX load='1m11' size='340' side='right' viewer='molstar' caption='[[1m11]], [[Resolution|resolution]] 16.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1m11]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/E7 E7] and [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M11 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M11 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1m11]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Echovirus_E7 Echovirus E7] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M11 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M11 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1g40|1g40]], [[1cov|1cov]], [[1ev1|1ev1]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 16&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m11 OCA], [https://pdbe.org/1m11 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m11 RCSB], [https://www.ebi.ac.uk/pdbsum/1m11 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m11 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m11 OCA], [https://pdbe.org/1m11 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m11 RCSB], [https://www.ebi.ac.uk/pdbsum/1m11 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m11 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/Q914E0_9ENTO Q914E0_9ENTO]] Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).[SAAS:SAAS000199_004_016611] Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease (By similarity).[SAAS:SAAS000199_004_042266] RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).[SAAS:SAAS000199_004_010047] [[https://www.uniprot.org/uniprot/DAF_HUMAN DAF_HUMAN]] This protein recognizes C4b and C3b fragments that condense with cell-surface hydroxyl or amino groups when nascent C4b and C3b are locally generated during C4 and c3 activation. Interaction of daf with cell-associated C4b and C3b polypeptides interferes with their ability to catalyze the conversion of C2 and factor B to enzymatically active C2a and Bb and thereby prevents the formation of C4b2a and C3bBb, the amplification convertases of the complement cascade.<ref>PMID:7525274</ref>
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[https://www.uniprot.org/uniprot/DAF_HUMAN DAF_HUMAN] This protein recognizes C4b and C3b fragments that condense with cell-surface hydroxyl or amino groups when nascent C4b and C3b are locally generated during C4 and c3 activation. Interaction of daf with cell-associated C4b and C3b polypeptides interferes with their ability to catalyze the conversion of C2 and factor B to enzymatically active C2a and Bb and thereby prevents the formation of C4b2a and C3bBb, the amplification convertases of the complement cascade.<ref>PMID:7525274</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1m11 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1m11 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Echoviruses are enteroviruses that belong to Picornaviridae. Many echoviruses use decay-accelerating factor (DAF) as their cellular receptor. DAF is a glycosylphosphatidyl inositol-anchored complement regulatory protein found on most cell surfaces. It functions to protect cells from complement attack. The cryo-electron microscopy reconstructions of echovirus 7 complexed with DAF show that the DAF-binding regions are located close to the icosahedral twofold axes, in contrast to other enterovirus complexes where the viral canyon is the receptor binding site. This novel receptor binding position suggests that DAF is important for the attachment of viral particles to host cells, but probably not for initiating viral uncoating, as is the case with canyon-binding receptors. Thus, a different cell entry mechanism must be used for enteroviruses that bind DAF.
 
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Structure of decay-accelerating factor bound to echovirus 7: a virus-receptor complex.,He Y, Lin F, Chipman PR, Bator CM, Baker TS, Shoham M, Kuhn RJ, Medof ME, Rossmann MG Proc Natl Acad Sci U S A. 2002 Aug 6;99(16):10325-9. Epub 2002 Jul 15. PMID:12119400<ref>PMID:12119400</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1m11" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
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__TOC__
__TOC__
</SX>
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[[Category: E7]]
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[[Category: Echovirus E7]]
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Baker, T S]]
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[[Category: Baker TS]]
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[[Category: Bator, C M]]
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[[Category: Bator CM]]
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[[Category: Chipman, P R]]
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[[Category: Chipman PR]]
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[[Category: He, Y]]
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[[Category: He Y]]
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[[Category: Kuhn, R J]]
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[[Category: Kuhn RJ]]
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[[Category: Lin, F]]
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[[Category: Lin F]]
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[[Category: Medof, M E]]
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[[Category: Medof ME]]
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[[Category: Rossmann, M G]]
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[[Category: Rossmann MG]]
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[[Category: Shoham, M]]
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[[Category: Shoham M]]
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[[Category: Decay-accelerating factor]]
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[[Category: Icosahedral virus]]
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[[Category: Scr]]
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[[Category: Virus-receptor complex]]
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Current revision

structural model of human decay-accelerating factor bound to echovirus 7 from cryo-electron microscopy

1m11, resolution 16.00Å

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