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Compression of functional space in HLA-A sequence diversity.

Zhao, Bing; Png, Adrian Eak H; Ren, Ee Chee; Kolatkar, Prasanna R; Mathura, Venkatarajan Subramaniam; Sakharkar, Meena Kishore; Kangueane, Pandjassarame.
Hum Immunol ; 64(7): 718-28, 2003 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-12826374
The major histocompatibility complex (MHC) is highly polymorphic and more than 1500 human MHC alleles are known to date. These alleles do not bind to a given peptide with identical affinity. Although MHC alleles are functionally related, it is difficult to quantify the functional variation between them. Three-dimensional structures of known MHC-peptide (MHCp) complexes suggest that specific peptide residues bind selectively to functional pockets in the binding groove. From a set of known MHCp structures we identified 21 critical polymorphic functional residue positions (CPFRP) that significantly reduced functional pocket variability to just 189 among 212 HLA-A alleles. Interestingly 101 HLA-A alleles clustered into 29 clusters such that the six functional pockets formed by the CPFRPs are identical within the cluster.