Compression of functional space in HLA-A sequence diversity

Bing Zhao, Adrian Eak H. Png, Ee Chee Ren, Prasanna R. Kolatkar, Venkatarajan Subramaniam Mathura, Meena Kishore Sakharkar, Pandjassarame Kangueane*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

22 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)718-728
Number of pages11
JournalHuman Immunology
Volume64
Issue number7
DOIs
Publication statusPublished - 1 Jul 2003
Externally publishedYes

Keywords

  • Functional pocket
  • MHC
  • Peptide binding

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