1P1Z

X-RAY CRYSTAL STRUCTURE OF THE LECTIN-LIKE NATURAL KILLER CELL RECEPTOR LY-49C BOUND TO ITS MHC CLASS I LIGAND H-2Kb

1P1Z の概要

• エントリーDOI: 10.2210/pdb1p1z/pdb
• 関連するPDBエントリー: 1JA3 1QO3
• 分子名称: H-2 class I histocompatibility antigen, K-B alpha chain, Beta-2-microglobulin, Ovalbumin peptide, ... (4 entities in total)
• 機能のキーワード: nk, kb, mhc, antigenic peptide, ly49, ova, immune system
• 由来する生物種: Mus musculus (house mouse); 詳細
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P01901; Secreted: P01887 P01012; Membrane; Single-pass type II membrane protein: Q64329
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 58686.60

構造登録者

Dimasi, N.,Natarajan, K.,Rangjin, G.,Dam, J.,Margulies, D.H.,Mariuzza, R.A. (登録日: 2003-04-14, 公開日: 2003-11-11, 最終更新日: 2024-10-16)

主引用文献

Dam, J.,Guan, R.,Natarajan, K.,Dimasi, N.,Chlewicki, L.K.,Kranz, D.M.,Schuck, P.,Margulies, D.H.,Mariuzza, R.A.
Variable MHC class I engagement by Ly49 natural killer cell receptors demonstrated by the crystal structure of Ly49C bound to H-2K(b).
Nat.Immunol., 4:1213-1222, 2003

PubMed Abstract: The Ly49 family of natural killer (NK) receptors regulates NK cell function by sensing major histocompatibility complex (MHC) class I. Ly49 receptors show complex patterns of MHC class I cross-reactivity and, in certain cases, peptide selectivity. To investigate whether specificity differences result from topological differences in MHC class I engagement, we determined the structure of the peptide-selective receptor Ly49C in complex with H-2K(b). The Ly49C homodimer binds two MHC class I molecules in symmetrical way, a mode distinct from that of Ly49A, which binds MHC class I asymmetrically. Ly49C does not directly contact the MHC-bound peptide. In addition, MHC crosslinking by Ly49C was demonstrated in solution. We propose a dynamic model for Ly49-MHC class I interactions involving conformational changes in the receptor, whereby variations in Ly49 dimerization mediate different MHC-binding modes.

PubMed: 14595439
DOI: 10.1038/ni1006

実験手法

X-RAY DIFFRACTION (3.26 Å)