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PDBsum entry 5b38
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Immune system
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PDB id
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5b38
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Contents |
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275 a.a.
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99 a.a.
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273 a.a.
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PDB id:
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Immune system
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Title:
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Kir3dl1 005 In complex with hla-b 57:01
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Structure:
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Hla class i histocompatibility antigen, b-57 alpha chain. Chain: a. Fragment: unp residues 25-300. Synonym: hla-b 57:01,Bw-57,mhc class i antigen b 57. Engineered: yes. Beta-2-microglobulin. Chain: b. Engineered: yes. Peptide from ig kappa chain c region.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: hla-b, hlab. Expressed in: enterobacteria phage l1. Expression_system_taxid: 268588. Gene: b2m, cdabp0092, hdcma22p. Synthetic: yes. Gene: kir3dl1, cd158e, nkat3, nkb1.
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Resolution:
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2.30Å
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R-factor:
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0.198
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R-free:
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0.251
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Authors:
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J.P.Vivian,J.Rossjohn
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Key ref:
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P.M.Saunders
et al.
(2016).
Killer cell immunoglobulin-like receptor 3DL1 polymorphism defines distinct hierarchies of HLA class I recognition.
J Exp Med,
213,
791-807.
PubMed id:
DOI:
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Date:
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12-Feb-16
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Release date:
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30-Mar-16
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PROCHECK
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Headers
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References
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P01889
(1B07_HUMAN) -
HLA class I histocompatibility antigen, B alpha chain from Homo sapiens
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Seq: Struc:
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362 a.a.
275 a.a.*
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DOI no:
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J Exp Med
213:791-807
(2016)
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PubMed id:
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Killer cell immunoglobulin-like receptor 3DL1 polymorphism defines distinct hierarchies of HLA class I recognition.
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P.M.Saunders,
P.Pymm,
G.Pietra,
V.A.Hughes,
C.Hitchen,
G.M.O'Connor,
F.Loiacono,
J.Widjaja,
D.A.Price,
M.Falco,
M.C.Mingari,
L.Moretta,
D.W.McVicar,
J.Rossjohn,
A.G.Brooks,
J.P.Vivian.
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ABSTRACT
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Natural killer (NK) cells play a key role in immunity, but how HLA class I
(HLA-I) and killer cell immunoglobulin-like receptor 3DL1 (KIR3DL1) polymorphism
impacts disease outcome remains unclear. KIR3DL1 (*001/*005/*015) tetramers were
screened for reactivity against a panel of HLA-I molecules. This revealed
different and distinct hierarchies of specificity for each KIR3DL1 allotype,
with KIR3DL1*005 recognizing the widest array of HLA-I ligands. These
differences were further reflected in functional studies using NK clones
expressing these specific KIR3DL1 allotypes. Unexpectedly, the Ile/Thr80
dimorphism in the Bw4-motif did not categorically define strong/weak KIR3DL1
recognition. Although the KIR3DL1*001, *005, and *015 polymorphisms are remote
from the KIR3DL1-HLA-I interface, the structures of these three KIR3DL1-HLA-I
complexes showed that the broader HLA-I specificity of KIR3DL1*005 correlated
with an altered KIR3DL1*005 interdomain positioning and increased mobility
within its ligand-binding site. Collectively, we provide a generic framework for
understanding the impact of KIR3DL1 polymorphism on the recognition of HLA-I
allomorphs.
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');
}
}
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