View source for 2m7w

==Independently verified structure of gp41-M-MAT, a membrane associated MPER trimer from HIV-1 gp41==
<StructureSection load='2m7w' size='340' side='right' caption='[[2m7w]], [[NMR_Ensembles_of_Models | 18 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2m7w]] 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=2M7W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2M7W FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2lp7|2lp7]]</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=2m7w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m7w OCA], [http://pdbe.org/2m7w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2m7w RCSB], [http://www.ebi.ac.uk/pdbsum/2m7w PDBsum]</span></td></tr>
</table>
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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Donald, B R]]
[[Category: Haynes, B F]]
[[Category: Martin, J W]]
[[Category: Moses, D S]]
[[Category: Munir, A S]]
[[Category: Reardon, P N]]
[[Category: Sage, H S]]
[[Category: Spicer, L D]]
[[Category: Gp41]]
[[Category: Mper]]
[[Category: Viral protein]]