4en2: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4en2]] 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=4EN2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EN2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4en2]] 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=4EN2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EN2 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=4en2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4en2 OCA], [https://pdbe.org/4en2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4en2 RCSB], [https://www.ebi.ac.uk/pdbsum/4en2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4en2 ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.58&#8491;</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=4en2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4en2 OCA], [https://pdbe.org/4en2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4en2 RCSB], [https://www.ebi.ac.uk/pdbsum/4en2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4en2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/AP1M1_MOUSE AP1M1_MOUSE]] Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the trans-Golgi network (TGN) and endosomes. The AP complexes mediate the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules.
[https://www.uniprot.org/uniprot/AP1M1_MOUSE AP1M1_MOUSE] Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the trans-Golgi network (TGN) and endosomes. The AP complexes mediate the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules.
<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 4en2" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Adaptin 3D structures|Adaptin 3D structures]]
*[[Adaptin 3D structures|Adaptin 3D structures]]
*[[Protein Nef|Protein Nef]]
*[[Protein Nef 3D structures|Protein Nef 3D structures]]
== References ==
<references/>
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</StructureSection>
</StructureSection>
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