Article ; Online: Structural Differences in KIR3DL1 and LILRB1 Interaction with HLA-B and the Loading Peptide Polymorphisms
Computational Biology Journal , Vol
In Silico Evidences
2015 Volume 2015
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 ... ...
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. |
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Keywords | Biology (General) ; QH301-705.5 |
Language | English |
Publishing date | 2015-01-01T00:00:00Z |
Publisher | Hindawi Publishing Corporation |
Document type | Article ; Online |
Database | BASE - Bielefeld Academic Search Engine (life sciences selection) |
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