Structural Differences in KIR3DL1 and LILRB1 Interaction with HLA-B and the Loading Peptide Polymorphisms:In SilicoEvidences | Zendy

Alba Grifoni | Zendy; Atanas Patronov | Zendy; Carla Montesano | Zendy; Vittorio Colizzi | Zendy; Massimo Amicosante | Zendy

Open Access

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

Author(s) -

Alba Grifoni,

Atanas Patronov,

Carla Montesano,

Vittorio Colizzi,

Massimo Amicosante

Publication year - 2015

Publication title -

computational biology journal

Language(s) - English

Resource type - Journals

eISSN - 2314-4173

pISSN - 2314-4165

DOI - 10.1155/2015/427217

Subject(s) - human leukocyte antigen , in silico , haplotype , allele , peptide , hla b antigens , genetics , epitope , amino acid , major histocompatibility complex , biology , chemistry , gene , biochemistry , antigen

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

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