View source for 4emz


==HIV-1 Nef in complex with MHC-I cytoplasmic domain and Mu1 adaptin subunit of AP1 adaptor (second domain)==
<StructureSection load='4emz' size='340' side='right'caption='[[4emz]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4emz]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EMZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EMZ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4emz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4emz OCA], [https://pdbe.org/4emz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4emz RCSB], [https://www.ebi.ac.uk/pdbsum/4emz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4emz ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/Q90VU7_9HIV1 Q90VU7_9HIV1]] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The HIV-1 protein Nef inhibits antigen presentation by class I major histocompatibility complex (MHC-I). We determined the mechanism of this activity by solving the crystal structure of a protein complex comprising Nef, the MHC-I cytoplasmic domain (MHC-I CD) and the mu1 subunit of the clathrin adaptor protein complex 1. A ternary, cooperative interaction clamps the MHC-I CD into a narrow binding groove at the Nef-mu1 interface, which encompasses the cargo-recognition site of mu1 and the proline-rich strand of Nef. The Nef C terminus induces a previously unobserved conformational change in mu1, whereas the N terminus binds the Nef core to position it optimally for complex formation. Positively charged patches on mu1 recognize acidic clusters in Nef and MHC-I. The structure shows how Nef functions as a clathrin-associated sorting protein to alter the specificity of host membrane trafficking and enable viral evasion of adaptive immunity.

Structural basis of evasion of cellular adaptive immunity by HIV-1 Nef.,Jia X, Singh R, Homann S, Yang H, Guatelli J, Xiong Y Nat Struct Mol Biol. 2012 Jun 17;19(7):701-6. doi: 10.1038/nsmb.2328. PMID:22705789<ref>PMID:22705789</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4emz" style="background-color:#fffaf0;"></div>

==See Also==
*[[Adaptin 3D structures|Adaptin 3D structures]]
*[[Protein Nef|Protein Nef]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Human immunodeficiency virus 1]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Jia X]]
[[Category: Xiong Y]]