4nee | pdb_00004nee
From Proteopedia
crystal structure of AP-2 alpha/simga2 complex bound to HIV-1 Nef
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Structural highlights
Publication Abstract from PubMedThe Nef protein of HIV-1 downregulates the cell surface co-receptor CD4 by hijacking the clathrin adaptor complex AP-2. The structural basis for the hijacking of AP-2 by Nef is revealed by a 2.9 A crystal structure of Nef bound to the alpha and sigma2 subunits of AP-2. Nef binds to AP-2 via its central loop (residues 149-179) and its core. The determinants for Nef binding include residues that directly contact AP-2 and others that stabilize the binding-competent conformation of the central loop. Residues involved in both direct and indirect interactions are required for the binding of Nef to AP-2 and for downregulation of CD4. These results lead to a model for the docking of the full AP-2 tetramer to membranes as bound to Nef, such that the cytosolic tail of CD4 is situated to interact with its binding site on Nef. DOI: https://dx.doi.org/10.7554/eLife.01754.001. How HIV-1 Nef hijacks the AP-2 clathrin adaptor to downregulate CD4.,Ren X, Park SY, Bonifacino JS, Hurley JH Elife. 2014;3:e01754. doi: 10.7554/eLife.01754. Epub 2014 Jan 1. PMID:24473078[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 13:38, 18 May 2014.