1DDH

MHC CLASS I H-2DD HEAVY CHAIN COMPLEXED WITH BETA-2 MICROGLOBULIN AND AN IMMUNODOMINANT PEPTIDE P18-I10 FROM THE HUMAN IMMUNODEFICIENCY VIRUS ENVELOPE GLYCOPROTEIN 120

1DDH の概要

• エントリーDOI: 10.2210/pdb1ddh/pdb
• 分子名称: MHC CLASS I H-2DD HEAVY CHAIN, BETA-2 MICROGLOBULIN, HUMAN IMMUNODEFICIENCY VIRUS ENVELOPE GLYCOPROTEIN 120, ... (4 entities in total)
• 機能のキーワード: complex (histocompatibility-antigen), histocompatibility antigen, class i major histocompatibility complex, mhc i, complex (histocompatibility-antigen) complex, complex (histocompatibility/antigen)
• 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: P01900; Secreted: P01887; Transmembrane protein gp41: Virion membrane; Single-pass type I membrane protein. Surface protein gp120: Virion membrane; Peripheral membrane protein: P04582
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 44616.06

構造登録者

Li, H.,Margulies, D.H.,Mariuzza, R.A. (登録日: 1998-06-22, 公開日: 1999-01-13, 最終更新日: 2024-10-23)

主引用文献

Li, H.,Natarajan, K.,Malchiodi, E.L.,Margulies, D.H.,Mariuzza, R.A.
Three-dimensional structure of H-2Dd complexed with an immunodominant peptide from human immunodeficiency virus envelope glycoprotein 120.
J.Mol.Biol., 283:179-191, 1998

PubMed Abstract: The crystal structure of the mouse major histocompatibility complex (MHC) class I molecule H-2Dd with an immunodominant peptide, designated P18-I10 (RGPGRAFVTI), from human immunodeficiency virus envelope glycoprotein 120 was determined at 3.2 A resolution. A novel orientation of the alpha3 domain of Dd relative to the alpha1/alpha2 domains results in significantly fewer contacts between alpha3 and beta2-microglobulin compared with other MHC class I proteins. Four out of ten peptide residues (P2 Gly, P3 Pro, P5 Arg and P10 Ile) are nearly completely buried in the Dd binding groove. This is consistent with previous findings that Dd exploits a four-residue binding motif comprising a glycine at P2, a proline at P3, a positively charged residue at P5, and a C-terminal hydrophobic residue at P9 or P10. The side-chain of P5 Arg is directed toward the floor of the predominantly hydrophobic binding groove where it forms two salt bridges and one hydrogen bond with Dd residue Asp77. The selection of glycine at P2 appears to be due to a narrowing of the B pocket, relative to that of other class I molecules, caused by Arg66 whose side-chain folds down into the binding cleft. Residue P3 Pro of P18-I10 occupies part of pocket D, which in Dd is partially split by a prominent hydrophobic ridge in the floor of the binding groove formed by Trp97 and Trp114. Residues P6 through P9 form a solvent-exposed bulge, with P7 Phe protruding the most from the binding groove and thereby probably constituting a major site of interaction with T cell receptors. A comparison of H-2Dd/P18-I10 with other MHC class I/peptide complexes of known structure provides insights into the possible basis for the specificity of the natural killer cell receptor Ly-49A for several related class I molecules.

PubMed: 9761682
DOI: 10.1006/jmbi.1998.2091

実験手法

X-RAY DIFFRACTION (3.1 Å)