Structural highlights
Function
[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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jia X, Singh R, Homann S, Yang H, Guatelli J, Xiong Y. Structural basis of evasion of cellular adaptive immunity by HIV-1 Nef. Nat Struct Mol Biol. 2012 Jun 17;19(7):701-6. doi: 10.1038/nsmb.2328. PMID:22705789 doi:10.1038/nsmb.2328
