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Title: Compression of functional space in HLA-A sequence diversity
Authors: Zhao, B.
Sakharkar, M.K. 
Kangueane, P.
Png, A.E.H.
Ren, E.C. 
Kolatkar, P.R. 
Mathura, V.S.
Keywords: Functional pocket
Peptide binding
Issue Date: 2003
Citation: Zhao, B., Sakharkar, M.K., Kangueane, P., Png, A.E.H., Ren, E.C., Kolatkar, P.R., Mathura, V.S. (2003). Compression of functional space in HLA-A sequence diversity. Human Immunology 64 (7) : 718-728. ScholarBank@NUS Repository.
Abstract: 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. © American Society for Histocompatibility and Immunogenetics, 2003. Published by Elsevier Inc.
Source Title: Human Immunology
ISSN: 01988859
DOI: 10.1016/S0198-8859(03)00078-8
Appears in Collections:Staff Publications

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