2lp7: Difference between revisions
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==Structure of gp41-M-MAT, a membrane associated MPER trimer from HIV-1 gp41.== | |||
<StructureSection load='2lp7' size='340' side='right' caption='[[2lp7]], [[NMR_Ensembles_of_Models | 11 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2lp7]] 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=2LP7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LP7 FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lp7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lp7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lp7 RCSB], [http://www.ebi.ac.uk/pdbsum/2lp7 PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The membrane proximal external region (MPER) of HIV-1 glycoprotein (gp) 41 is involved in viral-host cell membrane fusion. It contains short amino acid sequences that are binding sites for the HIV-1 broadly neutralizing antibodies 2F5, 4E10, and 10E8, making these binding sites important targets for HIV-1 vaccine development. We report a high-resolution structure of a designed MPER trimer assembled on a detergent micelle. The NMR solution structure of this trimeric domain, designated gp41-M-MAT, shows that the three MPER peptides each adopt symmetric alpha-helical conformations exposing the amino acid side chains of the antibody binding sites. The helices are closely associated at their N termini, bend between the 2F5 and 4E10 epitopes, and gradually separate toward the C termini, where they associate with the membrane. The mAbs 2F5 and 4E10 bind gp41-M-MAT with nanomolar affinities, consistent with the substantial exposure of their respective epitopes in the trimer structure. The traditional structure determination of gp41-M-MAT using the Xplor-NIH protocol was validated by independently determining the structure using the DISCO sparse-data protocol, which exploits geometric arrangement algorithms that guarantee to compute all structures and assignments that satisfy the data. | |||
Structure of an HIV-1-neutralizing antibody target, the lipid-bound gp41 envelope membrane proximal region trimer.,Reardon PN, Sage H, Dennison SM, Martin JW, Donald BR, Alam SM, Haynes BF, Spicer LD Proc Natl Acad Sci U S A. 2014 Jan 28;111(4):1391-6. doi:, 10.1073/pnas.1309842111. Epub 2014 Jan 13. PMID:24474763<ref>PMID:24474763</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: 9hiv1]] | [[Category: 9hiv1]] | ||
[[Category: Reardon, P N.]] | [[Category: Reardon, P N.]] | ||
[[Category: Gp41]] | [[Category: Gp41]] | ||
[[Category: Viral protein]] | [[Category: Viral protein]] | ||
Revision as of 12:51, 18 May 2014
Structure of gp41-M-MAT, a membrane associated MPER trimer from HIV-1 gp41.
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