View source for 2nct


==NMR assignment and structure of a peptide derived from the membrane proximal external region of HIV-1 gp41 in the presence of hexafluoroisopropanol==
<StructureSection load='2nct' size='340' side='right'caption='[[2nct]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2nct]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NCT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NCT FirstGlance]. <br>
</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=2nct FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nct OCA], [https://pdbe.org/2nct PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nct RCSB], [https://www.ebi.ac.uk/pdbsum/2nct PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nct ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q66X49_9HIV1 Q66X49_9HIV1] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The mechanism by which the HIV-1 MPER epitope is recognized by the potent neutralizing antibody 10E8 at membrane interfaces remains poorly understood. To solve this problem, we have optimized a 10E8 peptide epitope and analyzed the structure and binding activities of the antibody in membrane and membrane-like environments. The X-ray crystal structure of the Fab-peptide complex in detergents revealed for the first time that the epitope of 10E8 comprises a continuous helix spanning the gp41 MPER/transmembrane domain junction (MPER-N-TMD; Env residues 671-687). The MPER-N-TMD helix projects beyond the tip of the heavy-chain complementarity determining region 3 loop, indicating that the antibody sits parallel to the plane of the membrane in binding the native epitope. Biophysical, biochemical and mutational analyses demonstrated that strengthening the affinity of 10E8 for the TMD helix in a membrane environment, correlated with its neutralizing potency. Our research clarifies the molecular mechanisms underlying broad neutralization of HIV-1 by 10E8, and the structure of its natural epitope. The conclusions of our research will guide future vaccine-design strategies targeting MPER.

Structural basis for broad neutralization of HIV-1 through the molecular recognition of 10E8 helical epitope at the membrane interface.,Rujas E, Caaveiro JM, Partida-Hanon A, Gulzar N, Morante K, Apellaniz B, Garcia-Porras M, Bruix M, Tsumoto K, Scott JK, Jimenez MA, Nieva JL Sci Rep. 2016 Dec 1;6:38177. doi: 10.1038/srep38177. PMID:27905530<ref>PMID:27905530</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2nct" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Human immunodeficiency virus 1]]
[[Category: Large Structures]]
[[Category: Bruix M]]
[[Category: Jimenez M]]
[[Category: Nieva JL]]
[[Category: Partida-Hanon A]]
[[Category: Rujas E]]