6fy3: Difference between revisions
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<StructureSection load='6fy3' size='340' side='right' caption='[[6fy3]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='6fy3' size='340' side='right' caption='[[6fy3]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6fy3]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FY3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FY3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6fy3]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/9hiv1 9hiv1] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FY3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FY3 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=6fy3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fy3 OCA], [http://pdbe.org/6fy3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fy3 RCSB], [http://www.ebi.ac.uk/pdbsum/6fy3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fy3 ProSAT]</span></td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IGHV5-51 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), IGLV6-57 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), Env ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11676 9HIV1])</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=6fy3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fy3 OCA], [http://pdbe.org/6fy3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fy3 RCSB], [http://www.ebi.ac.uk/pdbsum/6fy3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fy3 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The alpha4beta7 integrin is a non-essential HIV-1 adhesion receptor, bound by the gp120 V1V2 domain, facilitating rapid viral dissemination into gut-associated lymphoid tissues. Antibodies blocking this interaction early in infection can improve disease outcome, and V1V2-targeted antibodies were correlated with moderate efficacy reported from the RV144 HIV-1 vaccine trial. Monoclonal alpha4beta7-blocking antibodies recognise two slightly different helical V2 conformations, and current structural data suggests their binding sites are occluded in prefusion envelope trimers. Here, we report cocrystal structures of two alpha4beta7-blocking antibodies from an infected donor complexed with scaffolded V1V2 or V2 peptides. Both antibodies recognised the same helix-coil V2 conformation as RV144 antibody CH58, identifying a frequently sampled alternative conformation of full-length V1V2. In the context of Envelope, this alpha-helical form of V1V2 displays highly exposed alpha4beta7-binding sites, potentially providing a functional role for non-native Envelope on virion or infected cell surfaces in HIV-1 dissemination, pathogenesis, and vaccine design. | |||
Common helical V1V2 conformations of HIV-1 Envelope expose the alpha4beta7 binding site on intact virions.,Wibmer CK, Richardson SI, Yolitz J, Cicala C, Arthos J, Moore PL, Morris L Nat Commun. 2018 Oct 26;9(1):4489. doi: 10.1038/s41467-018-06794-x. PMID:30367034<ref>PMID:30367034</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6fy3" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | |||
[[Category: Moore, P L]] | [[Category: Moore, P L]] | ||
[[Category: Morris, L]] | [[Category: Morris, L]] | ||
Latest revision as of 15:48, 7 November 2018
Crystal structure of a V2-directed, RV144 vaccine-like antibody from HIV-1 infection, CAP228-3D, bound to a heterologous V2 peptideCrystal structure of a V2-directed, RV144 vaccine-like antibody from HIV-1 infection, CAP228-3D, bound to a heterologous V2 peptide
Structural highlights
Publication Abstract from PubMedThe alpha4beta7 integrin is a non-essential HIV-1 adhesion receptor, bound by the gp120 V1V2 domain, facilitating rapid viral dissemination into gut-associated lymphoid tissues. Antibodies blocking this interaction early in infection can improve disease outcome, and V1V2-targeted antibodies were correlated with moderate efficacy reported from the RV144 HIV-1 vaccine trial. Monoclonal alpha4beta7-blocking antibodies recognise two slightly different helical V2 conformations, and current structural data suggests their binding sites are occluded in prefusion envelope trimers. Here, we report cocrystal structures of two alpha4beta7-blocking antibodies from an infected donor complexed with scaffolded V1V2 or V2 peptides. Both antibodies recognised the same helix-coil V2 conformation as RV144 antibody CH58, identifying a frequently sampled alternative conformation of full-length V1V2. In the context of Envelope, this alpha-helical form of V1V2 displays highly exposed alpha4beta7-binding sites, potentially providing a functional role for non-native Envelope on virion or infected cell surfaces in HIV-1 dissemination, pathogenesis, and vaccine design. Common helical V1V2 conformations of HIV-1 Envelope expose the alpha4beta7 binding site on intact virions.,Wibmer CK, Richardson SI, Yolitz J, Cicala C, Arthos J, Moore PL, Morris L Nat Commun. 2018 Oct 26;9(1):4489. doi: 10.1038/s41467-018-06794-x. PMID:30367034[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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