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New page: left|200px<br /> <applet load="2qzd" size="450" color="white" frame="true" align="right" spinBox="true" caption="2qzd" /> '''Fitted structure of SCR4 of DAF into cryoEM... |
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== | ==Fitted structure of SCR4 of DAF into cryoEM density== | ||
Many entero-, parecho-, and rhinoviruses use | <SX load='2qzd' size='340' side='right' viewer='molstar' caption='[[2qzd]], [[Resolution|resolution]] 14.00Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2qzd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QZD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QZD FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 14Å</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=2qzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qzd OCA], [https://pdbe.org/2qzd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qzd RCSB], [https://www.ebi.ac.uk/pdbsum/2qzd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qzd ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[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 == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qz/2qzd_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=2qzd ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Many entero-, parecho-, and rhinoviruses use immunoglobulin (Ig)-like receptors that bind into the viral canyon and are required to initiate viral uncoating during infection. However, some of these viruses use an alternative or additional receptor that binds outside the canyon. Both the coxsackievirus-adenovirus receptor (CAR), an Ig-like molecule that binds into the viral canyon, and decay-accelerating factor (DAF) have been identified as cellular receptors for coxsackievirus B3 (CVB3). A cryoelectron microscopy reconstruction of a variant of CVB3 complexed with DAF shows full occupancy of the DAF receptor in each of 60 binding sites. The DAF molecule bridges the canyon, blocking the CAR binding site and causing the two receptors to compete with one another. The binding site of DAF on CVB3 differs from the binding site of DAF on the surface of echoviruses, suggesting independent evolutionary processes. | |||
Interaction of decay-accelerating factor with coxsackievirus B3.,Hafenstein S, Bowman VD, Chipman PR, Bator Kelly CM, Lin F, Medof ME, Rossmann MG J Virol. 2007 Dec;81(23):12927-35. Epub 2007 Sep 5. PMID:17804498<ref>PMID:17804498</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2qzd" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[CD55|CD55]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</SX> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Bator Kelly CM]] | ||
[[Category: | [[Category: Bowman VD]] | ||
[[Category: | [[Category: Chipman PR]] | ||
[[Category: | [[Category: Hafenstein S]] | ||
[[Category: Lin | [[Category: Lin F]] | ||
[[Category: Medof | [[Category: Medof ME]] | ||
[[Category: Rossmann | [[Category: Rossmann MG]] | ||
Latest revision as of 08:28, 17 October 2024
Fitted structure of SCR4 of DAF into cryoEM densityFitted structure of SCR4 of DAF into cryoEM density
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