Allele effects in MHC-peptide interactions: a theoretical analysis of HLA-DRbeta1*0101-HA and HLA-DRbeta1*0401-HA complexes

Biochem Biophys Res Commun. 2005 May 20;330(4):1162-7. doi: 10.1016/j.bbrc.2005.03.102.

Abstract

HLA-DRbeta1*0101-HA and HLA-DRbeta1*0401-HA complexes are studied and compared by means of their computationally derived multipolar moments and electrostatic potentials. Changes in electrostatic potential are associated with definite pocket interaction profiles. Thus, Pocket 1 projects itself as an anchoring pocket for both complexes, in accordance with experimental results. While Pocket 4 has an anchoring profile in the HLA-DRbeta1*0101 allele, it presents itself as modulating pocket-peptide interactions in HLA-DRbeta1*0401. Pockets 6 and 7 both strongly contribute to allele specificity, with Pocket 7 being very important for HLA-DRbeta1*0401-HA. Pocket 9 acts as a "double purpose" interaction site for both alleles. It both projects itself as an anchoring pocket as well as modulating pocket-peptide interactions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alleles
  • Binding Sites
  • HLA-DR Antigens / chemistry*
  • HLA-DR Antigens / genetics
  • Hemagglutinin Glycoproteins, Influenza Virus
  • Hemagglutinins, Viral / chemistry*
  • Humans
  • Models, Molecular*
  • Peptide Fragments / chemistry*
  • Peptides / chemistry*
  • Static Electricity

Substances

  • HLA-DR Antigens
  • Hemagglutinin Glycoproteins, Influenza Virus
  • Hemagglutinins, Viral
  • Peptide Fragments
  • Peptides
  • influenza hemagglutinin (306-318)