6V3J

KIR3DL1 in complex with HLA-B*57:03 presenting the peptide LSSPVTKSF

6V3J の概要

• エントリーDOI: 10.2210/pdb6v3j/pdb
• 分子名称: HLA-B alpha chain (B*5703GB), Beta-2-microglobulin, Peptide Leu-Ser-Ser-Pro-Val-Thr-Lys-Ser-Phe, ... (6 entities in total)
• 機能のキーワード: peptide antigen, hla, mhc, immunity, immune system
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 78299.72

構造登録者

Maclachlan, B.,Rossjohn, J.,Vivian, J.P. (登録日: 2019-11-25, 公開日: 2020-05-20, 最終更新日: 2024-10-09)

主引用文献

Saunders, P.M.,MacLachlan, B.J.,Pymm, P.,Illing, P.T.,Deng, Y.,Wong, S.C.,Oates, C.V.L.,Purcell, A.W.,Rossjohn, J.,Vivian, J.P.,Brooks, A.G.
The molecular basis of how buried human leukocyte antigen polymorphism modulates natural killer cell function.
Proc.Natl.Acad.Sci.USA, 117:11636-11647, 2020

PubMed Abstract: Micropolymorphisms within human leukocyte antigen (HLA) class I molecules can change the architecture of the peptide-binding cleft, leading to differences in peptide presentation and T cell recognition. The impact of such HLA variation on natural killer (NK) cell recognition remains unclear. Given the differential association of HLA-B*57:01 and HLA-B*57:03 with the control of HIV, recognition of these HLA-B57 allomorphs by the killer cell immunoglobulin-like receptor (KIR) 3DL1 was compared. Despite differing by only two polymorphic residues, both buried within the peptide-binding cleft, HLA-B*57:01 more potently inhibited NK cell activation. Direct-binding studies showed KIR3DL1 to preferentially recognize HLA-B*57:01, particularly when presenting peptides with positively charged position (P)Ω-2 residues. In HLA-B*57:01, charged PΩ-2 residues were oriented toward the peptide-binding cleft and away from KIR3DL1. In HLA-B*57:03, the charged PΩ-2 residues protruded out from the cleft and directly impacted KIR3DL1 engagement. Accordingly, KIR3DL1 recognition of HLA class I ligands is modulated by both the peptide sequence and conformation, as determined by the HLA polymorphic framework, providing a rationale for understanding differences in clinical associations.

PubMed: 32404419
DOI: 10.1073/pnas.1920570117

実験手法

X-RAY DIFFRACTION (1.98 Å)