TITLE

Structural Differences in KIR3DL1 and LILRB1 Interaction with HLA-B and the Loading Peptide Polymorphisms: In Silico Evidences

AUTHOR(S)
Grifoni, Alba; Patronov, Atanas; Montesano, Carla; Colizzi, Vittorio; Amicosante, Massimo
PUB. DATE
November 2015
SOURCE
Computational Biology Journal;11/16/2015, p1
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
KIR3DL1 and LILRB1 interact with HLA class I. Using KIR3DL1/HLA-B interaction to set up the procedure, structural immune-informatics approaches have been performed in LILRB1/HLA-B alleles’ combination also considering the contribution of the HLA bound peptide. All KIR3DL1 alleles interact strongly with HLA-B alleles carrying Bw4 epitope and negative charged amino acid residues in peptide position P8 disrupt KIR3DL1 binding. HLA-B alleles carrying Ile 194 show a higher strength of interaction with LILRB1 in all the analyzed haplotypes. Finally, we hypothesize a contribution of the amino acid at position 1 of the HLA bound peptide in the modulation of HLA-B/LILRB1 interaction.
ACCESSION #
116637893

 

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