Compression of functional space in HLA-A sequence diversity

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

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21 Citations (Scopus)


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
Issue number7
Publication statusPublished - 1 Jul 2003
Externally publishedYes



  • Functional pocket
  • MHC
  • Peptide binding

ASJC Scopus subject areas

  • Immunology
  • Immunology and Allergy

Cite this

Zhao, B., Png, A. E. H., Ren, E. C., Kolatkar, P., Mathura, V. S., Sakharkar, M. K., & Kangueane, P. (2003). Compression of functional space in HLA-A sequence diversity. Human Immunology, 64(7), 718-728.