Structural highlights
Function
[Q90VU7_9HIV1]
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.
See Also
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
