4zkq: Difference between revisions
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The | ==Viral chemokine binding protein R17 encoded by rodent gammaherpesvirus Peru ( RHVP)== | ||
<StructureSection load='4zkq' size='340' side='right'caption='[[4zkq]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4zkq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cricetid_gammaherpesvirus_2 Cricetid gammaherpesvirus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZKQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZKQ FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.898Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=4zkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zkq OCA], [https://pdbe.org/4zkq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zkq RCSB], [https://www.ebi.ac.uk/pdbsum/4zkq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zkq ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/E9M5R0_9GAMA E9M5R0_9GAMA] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A wide variety of pathogens targets chemokine signaling networks in order to disrupt host immune surveillance and defense. Here, we report a structural and mutational analysis of rodent herpesvirus Peru encoded R17, a potent chemokine inhibitor that sequesters CC and C chemokines with high affinity. R17 consists of a pair of beta-sandwich domains linked together by a bridging sheet, which form an acidic binding cleft for the chemokine CCL3 on the opposite face of a basic surface cluster that binds glycosaminoglycans. R17 promiscuously engages chemokines primarily through the same N-loop determinants used for host receptor recognition while residues located in the chemokine 40s loop drive kinetically stable complex formation. The core fold adopted by R17 is unexpectedly similar to that of the M3 chemokine decoy receptor encoded by MHV-68, although, strikingly, neither the location of ligand engagement nor the stoichiometry of binding is conserved, suggesting that their functions evolved independently. | |||
Parallel Evolution of Chemokine Binding by Structurally Related Herpesvirus Decoy Receptors.,Lubman OY, Fremont DH Structure. 2015 Nov 30. pii: S0969-2126(15)00457-8. doi:, 10.1016/j.str.2015.10.018. PMID:26671708<ref>PMID:26671708</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Fremont | <div class="pdbe-citations 4zkq" style="background-color:#fffaf0;"></div> | ||
[[Category: Lubman | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Cricetid gammaherpesvirus 2]] | |||
[[Category: Large Structures]] | |||
[[Category: Fremont DH]] | |||
[[Category: Lubman OY]] | |||
Latest revision as of 11:41, 23 October 2024
Viral chemokine binding protein R17 encoded by rodent gammaherpesvirus Peru ( RHVP)Viral chemokine binding protein R17 encoded by rodent gammaherpesvirus Peru ( RHVP)
Structural highlights
FunctionPublication Abstract from PubMedA wide variety of pathogens targets chemokine signaling networks in order to disrupt host immune surveillance and defense. Here, we report a structural and mutational analysis of rodent herpesvirus Peru encoded R17, a potent chemokine inhibitor that sequesters CC and C chemokines with high affinity. R17 consists of a pair of beta-sandwich domains linked together by a bridging sheet, which form an acidic binding cleft for the chemokine CCL3 on the opposite face of a basic surface cluster that binds glycosaminoglycans. R17 promiscuously engages chemokines primarily through the same N-loop determinants used for host receptor recognition while residues located in the chemokine 40s loop drive kinetically stable complex formation. The core fold adopted by R17 is unexpectedly similar to that of the M3 chemokine decoy receptor encoded by MHV-68, although, strikingly, neither the location of ligand engagement nor the stoichiometry of binding is conserved, suggesting that their functions evolved independently. Parallel Evolution of Chemokine Binding by Structurally Related Herpesvirus Decoy Receptors.,Lubman OY, Fremont DH Structure. 2015 Nov 30. pii: S0969-2126(15)00457-8. doi:, 10.1016/j.str.2015.10.018. PMID:26671708[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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