1B0R

CRYSTAL STRUCTURE OF HLA-A*0201 COMPLEXED WITH A PEPTIDE WITH THE CARBOXYL-TERMINAL GROUP SUBSTITUTED BY A METHYL GROUP

1B0R の概要

• エントリーDOI: 10.2210/pdb1b0r/pdb
• 分子名称: PROTEIN (HLA-A*0201), PROTEIN (INFLUENZA MATRIX PEPTIDE) (3 entities in total)
• 機能のキーワード: hla-a2, antigenic peptides, class i mhc molecules, hla-a2 complexes, hydrogen bonds, protein structure, signaling protein
• 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: P01892; Secreted: P61769
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 44655.72

構造登録者

Bouvier, M.,Guo, H.,Smith, K.J.,Wiley, D.C. (登録日: 1998-11-12, 公開日: 1999-11-25, 最終更新日: 2024-10-30)

主引用文献

Bouvier, M.,Guo, H.C.,Smith, K.J.,Wiley, D.C.
Crystal structures of HLA-A*0201 complexed with antigenic peptides with either the amino- or carboxyl-terminal group substituted by a methyl group.
Proteins, 33:97-106, 1998

PubMed Abstract: The crystal structures of class I major histocompatibility complex (MHC) molecules complexed with antigenic peptides revealed a network of hydrogen bonds between the charged amino- and carboxyl-termini of the peptides and conserved MHC residues at both ends of the peptide binding site. These interactions were shown to contribute substantially to the stability of class I MHC/peptide complexes by thermal denaturation studies using synthetic peptides in which either the amino- or carboxyl-terminal group is substituted by a methyl group. Here we report crystal structures of HLA-A*0201 complexed with these terminally modified synthetic peptides showing that they adopt the same bound conformation as antigenic peptides. A number of variations in peptide conformation were observed for the terminally modified peptides, including in one case, a large conformational difference in four central peptide residues that is apparently caused by the lattice contact. This is reminiscent of the way binding a T-cell receptor changed the conformation of central residues of an MHC-bound peptide. The structures determined identify which conserved hydrogen bonds are eliminated in terminally substituted peptides and suggest an increased energetic importance of the interactions at the peptide termini for MHC-peptide stability.

PubMed: 9741848
DOI: 10.1002/(SICI)1097-0134(19981001)33:1<97::AID-PROT9>3.0.CO;2-I

実験手法

X-RAY DIFFRACTION (2.9 Å)