2HLA

SPECIFICITY POCKETS FOR THE SIDE CHAINS OF PEPTIDE ANTIGENS IN HLA-AW68

2HLA の概要

• エントリーDOI: 10.2210/pdb2hla/pdb
• 分子名称: CLASS I HISTOCOMPATIBILITY ANTIGEN (HLA-Aw68), BETA 2-MICROGLOBULIN (3 entities in total)
• 機能のキーワード: histocompatibility antigen
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P01891; Secreted . Note=(Microbial infection) In the presence of M: P61769
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 42899.49

構造登録者

Garrett, T.P.J.,Saper, M.A.,Wiley, D.C. (登録日: 1989-10-05, 公開日: 1990-04-15, 最終更新日: 2024-10-23)

主引用文献

Garrett, T.P.,Saper, M.A.,Bjorkman, P.J.,Strominger, J.L.,Wiley, D.C.
Specificity pockets for the side chains of peptide antigens in HLA-Aw68.
Nature, 342:692-696, 1989

PubMed Abstract: We have determined the structure of a second human histocompatibility glycoprotein, HLA-Aw68, by X-ray crystallography and refined it to a resolution of 2.6 A. Overall, the structure is extremely similar to that of HLA-A2 (refs 1, 2; and M.A.S. et al., manuscript in preparation), although the 11 amino-acid substitutions at polymorphic residues in the antigen-binding cleft alter the detailed shape and electrostatic charge of that site. A prominent negatively charged pocket within the cleft extends underneath the alpha-helix of the alpha 1-domain, providing a potential subsite for recognizing a positively charged side chain or peptide N terminus. Uninterpreted electron density, presumably representing an unknown 'antigen(s)', which seems to be different from that seen in the HLA-A2 structure, occupies the cleft and extends into the negatively charged pocket in HLA-Aw68. The structures of HLA-Aw68 and HLA-A2 demonstrate how polymorphism creates and alters subsites (pockets) positioned to bind peptide side chains, thereby suggesting the structural basis for allelic specificity in foreign antigen binding.

PubMed: 2594067
DOI: 10.1038/342692a0

実験手法

X-RAY DIFFRACTION (2.6 Å)