About: Structural Basis of Evasion of Cellular Adaptive Immunity by HIV-1 Nef

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An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Structural Basis of Evasion of Cellular Adaptive Immunity by HIV-1 Nef
Source	Medline; PMC
abstract	The HIV-1 protein Nef inhibits antigen presentation by class I MHC (MHC-I). Here the mechanism of this activity is revealed by the crystal structure of a protein complex consisting of Nef, the MHC-I cytoplasmic domain (MHC-I CD), and the μ1 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-μ1 interface encompassing the cargo-recognition site of μ1 and the proline rich strand of Nef. The Nef C-terminus induces a novel conformational change in μ1, while the N-terminus binds the Nef core to position it optimally for complex formation. Positively charged patches on μ1 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.
has issue date	2012-06-17(xsd:dateTime)
bibo:doi	10.1038/nsmb.2328
bibo:pmid	22705789
has license	no-cc
sha1sum (hex)	4ac06d96e9274c53d936ec2e59d5d46a7b54095c
schema:url	https://doi.org/10.1038/nsmb.2328
resource representing a document's title	Structural Basis of Evasion of Cellular Adaptive Immunity by HIV-1 Nef
has PubMed Central identifier	PMC3407041
has PubMed identifier	22705789
schema:publication	Nat Struct Mol Biol
resource representing a document's body	covid:4ac06d96e9274c53d936ec2e59d5d46a7b54095c#body_text
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