2AXH

Crystal structures of T cell receptor beta chains related to rheumatoid arthritis

2AXH の概要

• エントリーDOI: 10.2210/pdb2axh/pdb
• 分子名称: T cell receptor beta chain (2 entities in total)
• 機能のキーワード: tcr, immune system
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Membrane; Single-pass membrane protein (Potential): P01850
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 55214.55

構造登録者

Li, H.,Van Vranken, S.,Zhao, Y.,Li, Z.,Guo, Y.,Eisele, L.,Li, Y. (登録日: 2005-09-05, 公開日: 2005-09-20, 最終更新日: 2024-10-16)

主引用文献

Li, H.,Van Vranken, S.,Zhao, Y.,Li, Z.,Guo, Y.,Eisele, L.,Li, Y.
Crystal structures of T cell receptor (beta) chains related to rheumatoid arthritis.
Protein Sci., 14:3025-3038, 2005

PubMed Abstract: The crystal structures of the Vbeta17+ beta chains of two human T cell receptors (TCRs), originally derived from the synovial fluid (SF4) and tissue (C5-1) of a patient with rheumatoid arthritis (RA), have been determined in native (SF4) and mutant (C5-1(F104-->Y/C187-->S)) forms, respectively. These TCR beta chains form homo-dimers in solution and in crystals. Structural comparison reveals that the main-chain conformations in the CDR regions of the C5-1 and SF4 Vbeta17 closely resemble those of a Vbeta17 JM22 in a bound form; however, the CDR3 region shows different conformations among these three Vbeta17 structures. At the side-chain level, conformational differences were observed at the CDR2 regions between our two ligand-free forms and the bound JM22 form. Other significant differences were observed at the Vbeta regions 8-12, 40-44, and 82-88 between C5-1/SF4 and JM22 Vbeta17, implying that there is considerable variability in the structures of very similar beta chains. Structural alignments also reveal a considerable variation in the Vbeta-Cbeta associations, and this may affect ligand recognition. The crystal structures also provide insights into the structure basis of T cell recognition of Mycoplasma arthritidis mitogen (MAM), a superantigen that may be implicated in the development of human RA. Structural comparisons of the Vbeta domains of known TCR structures indicate that there are significant similarities among Vbeta regions that are MAM-reactive, whereas there appear to be significant structural differences among those Vbeta regions that lack MAM-reactivity. It further reveals that CDR2 and framework region (FR) 3 are likely to account for the binding of TCR to MAM.

PubMed: 16260763
DOI: 10.1110/ps.051748305

実験手法

X-RAY DIFFRACTION (2.7 Å)