1TVD

VARIABLE DOMAIN OF T CELL RECEPTOR DELTA CHAIN

1TVD の概要

• エントリーDOI: 10.2210/pdb1tvd/pdb
• 分子名称: T CELL RECEPTOR (2 entities in total)
• 機能のキーワード: immunoreceptor, tcr, delta chain, variable domain
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26291.25

構造登録者

Li, H.M.,Lebedeva, M.I.,Llera, A.S.,Fields, B.A.,Brenner, M.B.,Mariuzza, R.A. (登録日: 1997-10-19, 公開日: 1998-04-22, 最終更新日: 2024-11-13)

主引用文献

Li, H.,Lebedeva, M.I.,Llera, A.S.,Fields, B.A.,Brenner, M.B.,Mariuzza, R.A.
Structure of the Vdelta domain of a human gammadelta T-cell antigen receptor.
Nature, 391:502-506, 1998

PubMed Abstract: Antigen recognition by T lymphocytes is mediated by cell-surface glycoproteins known as T-cell antigen receptors (TCRs). These are composed of alpha and beta, or gamma and delta, polypeptide chains with variable (V) and constant (C) regions. In contrast to alphabeta TCRs, which recognize antigen only as peptide fragments bound to molecules of the major histocompatibility complex (MHC), gammadelta TCRs appear to recognize proteins directly, without antigen processing, and to recognize MHC molecules independently of the bound peptide. Moreover, small phosphate-containing non-peptide compounds have also been identified as ligands for certain gammadelta T cells. These studies indicate that antigen recognition by gammadelta TCRs may be fundamentally different from that by alphabeta TCRs. The three-dimensional structures of several alphabeta TCRs and TCR fragments, and their complexes with peptide-MHC or superantigens, have been determined. Here we report the crystal structure of the Vdelta domain of a human gammadelta TCR at 1.9 A resolution. A comparison with antibody and alphabeta TCR V domains reveals that the framework structure of Vdelta more closely resembles that of VH than of Valpha, Vbeta or VL (where H and L refer to heavy and light chains), whereas the relative positions and conformations of its complementarity-determining regions (CDRs) share features of both Valpha and VH. These results provide the first direct evidence that gammadelta TCRs are structurally distinct from alphabeta TCRs and, together with the observation that the CDR3 length distribution of TCR delta chains is similar to that of immunoglobulin heavy chains, are consistent with functional studies suggesting that recognition of certain antigens by gammadelta TCRs may resemble antigen recognition by antibodies.

PubMed: 9461220
DOI: 10.1038/35172

実験手法

X-RAY DIFFRACTION (1.9 Å)