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 language | English |
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Pages (from-to) | 718-728 |
Number of pages | 11 |
Journal | Human Immunology |
Volume | 64 |
Issue number | 7 |
DOIs | |
Publication status | Published - 1 Jul 2003 |
Externally published | Yes |
Keywords
- Functional pocket
- MHC
- Peptide binding