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PDBsum entry 5b38

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protein ligands Protein-protein interface(s) links
Immune system PDB id
5b38

 

 

 

 

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Contents
Protein chains
275 a.a.
99 a.a.
273 a.a.
Ligands
LEU-SER-SER-PRO-
VAL-THR-LYS-SER-
PHE
NAG ×3
Waters ×235
PDB id:
5b38
Name: Immune system
Title: Kir3dl1 005 In complex with hla-b 57:01
Structure: 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.
Source: 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.
Resolution:
2.30Å     R-factor:   0.198     R-free:   0.251
Authors: J.P.Vivian,J.Rossjohn
Key ref: 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: 27045007 DOI: 10.1084/jem.20152023
Date:
12-Feb-16     Release date:   30-Mar-16    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P01889  (1B07_HUMAN) -  HLA class I histocompatibility antigen, B alpha chain from Homo sapiens
Seq:
Struc:
362 a.a.
275 a.a.*
Protein chain
Pfam   ArchSchema ?
P61769  (B2MG_HUMAN) -  Beta-2-microglobulin from Homo sapiens
Seq:
Struc:
119 a.a.
99 a.a.
Protein chain
Pfam   ArchSchema ?
P43629  (KI3L1_HUMAN) -  Killer cell immunoglobulin-like receptor 3DL1 from Homo sapiens
Seq:
Struc:
444 a.a.
273 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 30 residue positions (black crosses)

 

 
DOI no: 10.1084/jem.20152023 J Exp Med 213:791-807 (2016)
PubMed id: 27045007  
 
 
Killer cell immunoglobulin-like receptor 3DL1 polymorphism defines distinct hierarchies of HLA class I recognition.
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.
 
  ABSTRACT  
 
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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