4zlt: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4zlt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cricetid_gammaherpesvirus_2 Cricetid gammaherpesvirus 2] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZLT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZLT FirstGlance]. <br> | <table><tr><td colspan='2'>[[4zlt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cricetid_gammaherpesvirus_2 Cricetid gammaherpesvirus 2] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZLT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZLT FirstGlance]. <br> | ||
</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> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</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=4zlt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zlt OCA], [https://pdbe.org/4zlt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zlt RCSB], [https://www.ebi.ac.uk/pdbsum/4zlt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zlt 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=4zlt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zlt OCA], [https://pdbe.org/4zlt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zlt RCSB], [https://www.ebi.ac.uk/pdbsum/4zlt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zlt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 11:20, 27 September 2023
Crystal structure of viral chemokine binding protein R17 in complex with CCL3Crystal structure of viral chemokine binding protein R17 in complex with CCL3
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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