6e8w: Difference between revisions
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<StructureSection load='6e8w' size='340' side='right' caption='[[6e8w]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | <StructureSection load='6e8w' size='340' side='right' caption='[[6e8w]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6e8w]] is a 3 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E8W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E8W FirstGlance]. <br> | <table><tr><td colspan='2'>[[6e8w]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/9hiv1 9hiv1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E8W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E8W 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=6e8w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e8w OCA], [http://pdbe.org/6e8w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e8w RCSB], [http://www.ebi.ac.uk/pdbsum/6e8w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e8w ProSAT]</span></td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">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=6e8w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e8w OCA], [http://pdbe.org/6e8w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e8w RCSB], [http://www.ebi.ac.uk/pdbsum/6e8w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e8w ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The membrane-proximal external region (MPER) of the HIV-1 envelope glycoprotein (Env) bears epitopes of broadly neutralizing antibodies (bnAbs) from infected individuals; it is thus a potential vaccine target. We report an NMR structure of the MPER and its adjacent transmembrane domain in bicelles that mimic a lipid-bilayer membrane. The MPER lies largely outside the lipid bilayer. It folds into a threefold cluster, stabilized mainly by conserved hydrophobic residues and potentially by interaction with phospholipid headgroups. Antigenic analysis and comparison with published images from electron cryotomography of HIV-1 Env on the virion surface suggest that the structure may represent a prefusion conformation of the MPER, distinct from the fusion-intermediate state targeted by several well-studied bnAbs. Very slow bnAb binding indicates that infrequent fluctuations of the MPER structure give these antibodies occasional access to alternative conformations of MPER epitopes. Mutations in the MPER not only impede membrane fusion but also influence presentation of bnAb epitopes in other regions. These results suggest strategies for developing MPER-based vaccine candidates. | |||
Structure of the membrane proximal external region of HIV-1 envelope glycoprotein.,Fu Q, Shaik MM, Cai Y, Ghantous F, Piai A, Peng H, Rits-Volloch S, Liu Z, Harrison SC, Seaman MS, Chen B, Chou JJ Proc Natl Acad Sci U S A. 2018 Sep 5. pii: 1807259115. doi:, 10.1073/pnas.1807259115. PMID:30185554<ref>PMID:30185554</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6e8w" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 23:21, 19 September 2018
MPER-TM Domain of HIV-1 envelope glycoprotein (Env)MPER-TM Domain of HIV-1 envelope glycoprotein (Env)
Structural highlights
Publication Abstract from PubMedThe membrane-proximal external region (MPER) of the HIV-1 envelope glycoprotein (Env) bears epitopes of broadly neutralizing antibodies (bnAbs) from infected individuals; it is thus a potential vaccine target. We report an NMR structure of the MPER and its adjacent transmembrane domain in bicelles that mimic a lipid-bilayer membrane. The MPER lies largely outside the lipid bilayer. It folds into a threefold cluster, stabilized mainly by conserved hydrophobic residues and potentially by interaction with phospholipid headgroups. Antigenic analysis and comparison with published images from electron cryotomography of HIV-1 Env on the virion surface suggest that the structure may represent a prefusion conformation of the MPER, distinct from the fusion-intermediate state targeted by several well-studied bnAbs. Very slow bnAb binding indicates that infrequent fluctuations of the MPER structure give these antibodies occasional access to alternative conformations of MPER epitopes. Mutations in the MPER not only impede membrane fusion but also influence presentation of bnAb epitopes in other regions. These results suggest strategies for developing MPER-based vaccine candidates. Structure of the membrane proximal external region of HIV-1 envelope glycoprotein.,Fu Q, Shaik MM, Cai Y, Ghantous F, Piai A, Peng H, Rits-Volloch S, Liu Z, Harrison SC, Seaman MS, Chen B, Chou JJ Proc Natl Acad Sci U S A. 2018 Sep 5. pii: 1807259115. doi:, 10.1073/pnas.1807259115. PMID:30185554[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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