PDBsum entry 4n8v

Immune system

PDB id: 4n8v

Contents

Protein chains

190 a.a.

274 a.a.

100 a.a.

Ligands

MET-LEU-ILE-TYR-SER-MET-TRP-GLY-LYS ×2

Waters ×124

PDB id:

4n8v

Name:

Immune system

Title:

Crystal structure of killer cell immunoglobulin-like receptor kir2ds2 in complex with hla-a

Structure:

Killer cell immunoglobulin-like receptor 2ds2. Chain: g, i. Fragment: unp residues 22-221. Synonym: kir2ds2. Engineered: yes. Hla class i histocompatibility antigen, a-11 alpha chain. Chain: a, d. Fragment: unp residues 25-298. Synonym: hla-a 11:01, Mhc class i antigen a 11.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: kir2ds2. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: hla-a. Gene: b2m. Synthetic: yes.

Resolution:

2.50Å R-factor: 0.224 R-free: 0.257

Authors:

J.X.Liu,E.C.Ren

Key ref:

J.Liu et al. (2014). Activating killer cell immunoglobulin-like receptor 2DS2 binds to HLA-A*11. Proc Natl Acad Sci U S A, 111, 2662-2667. PubMed id: 24550293 DOI: 10.1073/pnas.1322052111

Date:

18-Oct-13 Release date: 05-Feb-14

Protein chains

P43631  (KI2S2_HUMAN) -  Killer cell immunoglobulin-like receptor 2DS2 from Homo sapiens

Seq: 304 a.a.

Struc: 190 a.a.

Protein chains

P04439  (1A03_HUMAN) -  HLA class I histocompatibility antigen, A alpha chain from Homo sapiens

Seq: 365 a.a.

Struc: 274 a.a.*

Protein chains

P61769  (B2MG_HUMAN) -  Beta-2-microglobulin from Homo sapiens

Seq: 119 a.a.

Struc: 100 a.a.*

* PDB and UniProt seqs differ at 8 residue positions (black crosses)

DOI no: 10.1073/pnas.1322052111

Proc Natl Acad Sci U S A 111:2662-2667 (2014)

PubMed id: 24550293

Activating killer cell immunoglobulin-like receptor 2DS2 binds to HLA-A*11.

J.Liu, Z.Xiao, H.L.Ko, M.Shen, E.C.Ren.

ABSTRACT

Inhibitory killer cell Ig-like receptors (KIRs) are known to recognize HLA ligands mainly of the HLA-C and Bw4 groups, but the ligands for KIRs are poorly understood. We report here the identification of the cognate ligand for the activating KIR 2DS2 as HLA-A*11:01. The crystal structure of the KIR2DS2-HLA-A*11:01 complex was solved at 2.5-Å resolution and revealed residue-binding characteristics distinct from those of inhibitory KIRs with HLA-C and the critical role of residues Tyr45 and Asp72 in shaping binding specificity to HLA-A*11:01. Using KIR2DS2 tetramers, binding to surface HLA-A*11:01 on live cells was demonstrated and, furthermore, that binding can be altered by residue changes at p8 of the peptide, indicating the influence of peptide sequence on KIR-HLA association. In addition, heteronuclear single quantum coherence NMR was used to map the involvement of critical residues in HLA binding at the interface of KIR and HLA, and validates the data observed in the crystal structure. Our data provide structural evidence of the recognition of A*11:01 by the activating KIR2DS2 and extend our understanding of the KIR-HLA binding spectrum.