1g40: Difference between revisions
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<table cellpadding='5'><tr><td style='background-color: yellow;border:2px solid black;font-size:150%;'> | |||
WARNING: This structure was flagged as problematic. For additional information see '''2009, December:''' at [[Retractions and Fraud]].</td></tr></table> | |||
[[Image: | ==CRYSTAL STRUCTURE OF A COMPLEMENT PROTEIN THAT REGULATES BOTH PATHWAYS OF COMPLEMENT ACTIVATION AND BINDS HEPARAN SULFATE PROTEOGLYCANS== | ||
<StructureSection load='1g40' size='340' side='right' caption='[[1g40]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1g40]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Vaccinia_virus Vaccinia virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G40 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G40 FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g40 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g40 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1g40 RCSB], [http://www.ebi.ac.uk/pdbsum/1g40 PDBsum]</span></td></tr> | |||
</table> | |||
== 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/g4/1g40_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Vaccinia virus complement control protein (VCP) inhibits both pathways of complement activation through binding the third and fourth components. A homolog of mammalian regulators of complement activation, its ability to bind heparin endows VCP with additional activities of significance to viral infectivity. The structure of VCP reveals a highly extended molecule with a putative heparin recognition site at its C-terminal end. A second cluster of positive charges provides a possibly overlapping binding site for both heparin and complement components. Experiments suggested by the structure indicate that VCP can bind heparin and control complement simultaneously. This, the structure of any intact regulator of complement activation, along with attendant functional insights, will stimulate the design of new therapeutic inhibitors of complement. | |||
Crystal structure of a complement control protein that regulates both pathways of complement activation and binds heparan sulfate proteoglycans.,Murthy KH, Smith SA, Ganesh VK, Judge KW, Mullin N, Barlow PN, Ogata CM, Kotwal GJ Cell. 2001 Jan 26;104(2):301-11. PMID:11207370<ref>PMID:11207370</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | |||
*[[Retractions and Fraud|Retractions and Fraud]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
== | |||
< | |||
[[Category: Vaccinia virus]] | [[Category: Vaccinia virus]] | ||
[[Category: Barlow, P N | [[Category: Barlow, P N]] | ||
[[Category: Ganesh, V K | [[Category: Ganesh, V K]] | ||
[[Category: Judge, K W | [[Category: Judge, K W]] | ||
[[Category: Kotwal, G K | [[Category: Kotwal, G K]] | ||
[[Category: Mullin, N | [[Category: Mullin, N]] | ||
[[Category: Murthy, K H.M | [[Category: Murthy, K H.M]] | ||
[[Category: Ogata, C M | [[Category: Ogata, C M]] | ||
[[Category: Smith, S A | [[Category: Smith, S A]] | ||
[[Category: Beta]] | [[Category: Beta]] | ||
[[Category: Immune system]] | |||
[[Category: Module]] | [[Category: Module]] | ||
Revision as of 11:29, 18 November 2014
| WARNING: This structure was flagged as problematic. For additional information see 2009, December: at Retractions and Fraud. |
CRYSTAL STRUCTURE OF A COMPLEMENT PROTEIN THAT REGULATES BOTH PATHWAYS OF COMPLEMENT ACTIVATION AND BINDS HEPARAN SULFATE PROTEOGLYCANSCRYSTAL STRUCTURE OF A COMPLEMENT PROTEIN THAT REGULATES BOTH PATHWAYS OF COMPLEMENT ACTIVATION AND BINDS HEPARAN SULFATE PROTEOGLYCANS
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedVaccinia virus complement control protein (VCP) inhibits both pathways of complement activation through binding the third and fourth components. A homolog of mammalian regulators of complement activation, its ability to bind heparin endows VCP with additional activities of significance to viral infectivity. The structure of VCP reveals a highly extended molecule with a putative heparin recognition site at its C-terminal end. A second cluster of positive charges provides a possibly overlapping binding site for both heparin and complement components. Experiments suggested by the structure indicate that VCP can bind heparin and control complement simultaneously. This, the structure of any intact regulator of complement activation, along with attendant functional insights, will stimulate the design of new therapeutic inhibitors of complement. Crystal structure of a complement control protein that regulates both pathways of complement activation and binds heparan sulfate proteoglycans.,Murthy KH, Smith SA, Ganesh VK, Judge KW, Mullin N, Barlow PN, Ogata CM, Kotwal GJ Cell. 2001 Jan 26;104(2):301-11. PMID:11207370[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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