View source for 5vwl


==Solution NMR Structure of the Membrane Associated Segment of HIV-1 gp41 Cytoplasmic Tail==
<StructureSection load='5vwl' size='340' side='right'caption='[[5vwl]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5vwl]] 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=5VWL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VWL 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=5vwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vwl OCA], [https://pdbe.org/5vwl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vwl RCSB], [https://www.ebi.ac.uk/pdbsum/5vwl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vwl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q6TAN6_9HIV1 Q6TAN6_9HIV1] 
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== Publication Abstract from PubMed ==
The cytoplasmic tail of gp41 (gp41CT) remains the last HIV-1 domain with an unknown structure. It plays important roles in HIV-1 replication such as mediating envelope (Env) intracellular trafficking and incorporation into assembling virions, mechanisms of which are poorly understood. Here, we present the solution structure of gp41CT in a micellar environment and characterize its interaction with the membrane. We show that the N-terminal 45 residues are unstructured and not associated with the membrane. However, the C-terminal 105 residues form three membrane-bound amphipathic alpha helices with distinctive structural features such as variable degree of membrane penetration, hydrophobic and basic surfaces, clusters of aromatic residues, and a network of cation-pi interactions. This work fills a major gap by providing the structure of the last segment of HIV-1 Env, which will provide insights into the mechanisms of Gag-mediated Env incorporation as well as the overall Env mobility and conformation on the virion surface.

Solution Structure and Membrane Interaction of the Cytoplasmic Tail of HIV-1 gp41 Protein.,Murphy RE, Samal AB, Vlach J, Saad JS Structure. 2017 Oct 13. pii: S0969-2126(17)30301-5. doi:, 10.1016/j.str.2017.09.010. PMID:29056482<ref>PMID:29056482</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Gp41 3D Structures|Gp41 3D Structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Human immunodeficiency virus 1]]
[[Category: Large Structures]]
[[Category: Murphy RE]]
[[Category: Saad JS]]
[[Category: Samal A]]
[[Category: Vlach J]]