Allele effects in MHC-peptide interactions: a theoretical analysis of HLA-DRbeta10101-HA and HLA-DRbeta10401-HA complexes

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...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2005-05, Vol.330 (4), p.1162-1167
Main Authors: Cárdenas, Constanza, Ortiz, Marysol, Balbín, Alejandro, Villaveces, José Luis, Patarroyo, Manuel E
Format: Article
Language:English
Subjects:
Alleles
Binding Sites
Hemagglutinin Glycoproteins, Influenza Virus
Hemagglutinins, Viral - chemistry
HLA-DR Antigens - chemistry
HLA-DR Antigens - genetics
Humans
Models, Molecular
Peptide Fragments - chemistry
Peptides - chemistry
Static Electricity
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Summary: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.
ISSN:0006-291X