Correlated mutations in the HLA class II molecule

Anna M. Nilsson, Mihirinie Wijaywardene, George Gkoutos, Keith M. Wilson, Nelson Fernández, Christopher A. Reynolds

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)


A correlated mutation analysis was performed on aligned sequences of the human leukocyte antigen (HLA) HLA-DR, HLA-DP, and HLA-DQ class II receptors with a view to understanding their molecular associations, particularly those involving their α and β domains. The analysis was carried out on 23 HLA-DR alleles, 12 DP alleles, and 24 DQ alleles; the analysis was also carried out on the global alignment of the DR, DP, and DQ alleles. These analyses identified 13, 18, 26, and 27 correlated mutations, respectively. Between 72 and 85% of the correlated mutations were found to occur at domain interfaces within the α or β chain, at the interface of the αβ heterodimer, or at the interface of the (αβ)2 dimer of heterodimers. These results are discussed in the light of recent results that have shown that the HLA class II receptor forms temperature-dependent dimers of dimers on the surface of living cells.

Original languageEnglish
Pages (from-to)85-96
Number of pages12
JournalInternational Journal of Quantum Chemistry
Issue number2
Publication statusPublished - 30 Mar 1999
Externally publishedYes
EventISQBP President's Meeting: Molecular Structure and Dynamics in Biology - Elba, Italy
Duration: 8 Sep 199811 Sep 1998


  • Correlated mutation analysis
  • Dimers
  • Domain interfaces
  • Major histocompatibility receptor class II
  • Protein interfaces

ASJC Scopus subject areas

  • Atomic and Molecular Physics, and Optics
  • Condensed Matter Physics
  • Physical and Theoretical Chemistry


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