Table of Contents
Computational Biology Journal
Volume 2015, Article ID 427217, 10 pages
Research Article

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

1ProxAgen Ltd., 63 Shipchenski Prohod, 1574 Sofia, Bulgaria
2Department of Biology, University of Rome Tor Vergata, Via della Ricerca Scientifica 18, 00133 Rome, Italy
3Department of Biomedicine and Prevention, University of Rome Tor Vergata, Via Montpellier 1, 00133 Rome, Italy

Received 24 August 2015; Revised 21 October 2015; Accepted 26 October 2015

Academic Editor: Jinn Moon Yang

Copyright © 2015 Alba Grifoni et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


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.