2FWO

MHC Class I H-2Kd heavy chain in complex with beta-2microglobulin and peptide derived from influenza nucleoprotein

2FWO の概要

• エントリーDOI: 10.2210/pdb2fwo/pdb
• 分子名称: H-2 class I histocompatibility antigen, K-D alpha chain, Beta-2-microglobulin, TYQRTRALV peptide from Nucleoprotein, ... (4 entities in total)
• 機能のキーワード: mhc, antigens/peptides/epitopes, antigen processing/presentation, immune system-viral protein complex, immune system/viral protein
• 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: P01902; Secreted: P01887
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 45855.40

構造登録者

Mitaksov, V.,Fremont, D.H. (登録日: 2006-02-02, 公開日: 2006-02-21, 最終更新日: 2024-11-13)

主引用文献

Mitaksov, V.,Fremont, D.H.
Structural Definition of the H-2Kd Peptide-binding Motif.
J.Biol.Chem., 281:10618-10625, 2006

PubMed Abstract: Classic major histocompatibility complex (MHC) proteins associate with antigen- and self-derived peptides in an allele-specific manner. Herein we present the crystal structure of the MHC class I protein H-2K(d) (K(d)) expressed by BALB/c mice in complex with an antigenic peptide derived from influenza A/PR/8/34 nucleoprotein (Flu, residues 147-155, TYQRTRALV). Analysis of our structure in conjunction with the sequences of naturally processed epitopes provides a comprehensive understanding of the dominant K(d) peptide-binding motif. We find that Flu residues Tyr(P2), Thr(P5), and Val(P9) are sequestered into the B, C, and F pockets of the K(d) groove, respectively. The shape and chemistry of the polymorphic B pocket make it an optimal binding site for the side chain of Tyr(P2) as the dominant anchoring residue of nonameric peptides. The non-polar F pocket limits the amino acid repertoire at P9 to hydrophobic residues such as Ile, Leu, or Val, whereas the C pocket restricts the size of the P5-anchoring side chain. We also show that Flu is accommodated in the complex through an unfavorable kink in the otherwise extended peptide backbone due to the presence of a prominent ridge in the K(d) groove. Surprisingly, this backbone conformation is strikingly similar to D(b)-presented peptides despite the fact that these proteins employ distinct motif-anchoring strategies. The results presented in this study provide a solid foundation for the understanding of K(d)-restricted antigen presentation and recognition events.

PubMed: 16473882
DOI: 10.1074/jbc.M510511200

実験手法

X-RAY DIFFRACTION (2.6 Å)