Crystal structure of an isolated V(alpha) domain of the 2C T-cell receptor.
Crystal structure of an isolated V(alpha) domain of the 2C T-cell receptor.
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2C T 细胞受体的分离 V(α) 结构域的晶体结构。
DOI：
10.1006/jmbi.2001.5113
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发表时间：
2001
期刊：
影响因子：
--
通讯作者：
Wilson,IA
中科院分区：
文献类型：
--
作者：
Rudolph,MG;Huang,M;Teyton,L;Wilson,IA
T细胞受体是一种异源二聚体细胞表面蛋白，由α和β两条链组成，每条链由一个可变结构域(V)和一个恒定结构域(C)组成。从含有完整TCR2C和CD3CD3-α-链胞外区的溶液中偶然生长出小鼠TCR2C的V-γϵ结构域的晶体。V-α晶体结构显示了晶体堆积如何以不同于V-α/V-α同二聚体和V-α/V-α异质二聚体结构中观察到的方式替代另一个V-β结构域。在CDR3和β3β4环中发生显著的构象变化，这两个环通常构成二聚体界面的一部分。单体Vα结构域为研究二聚化对TCR的非连接互补决定区构象的影响提供了独特的机会。单个Vα模块的这种结构对分离的抗体和免疫球蛋白结构域的稳定性和生物工程具有重要意义。
The T-cell receptor (TCR) is a heterodimeric cell-surface protein consisting of two chains, α and β, each of which is composed of a variable (V) and a constant (C) domain. Crystals of the isolated Vαdomain of the murine TCR 2C were grown by serendipity from a solution containing the extracellular domains of the intact TCR 2C and CD3 γϵ-chains. The Vαcrystal structure shows how crystal packing can substitute for another Vαdomain in a different fashion from that observed in Vα/Vαhomodimer and Vα/Vβheterodimer structures. Significant conformational changes occur in the CDR3 and β3β4loops that normally form part of the dimer interface. The monomeric Vαdomain provides the unique opportunity to study the effect of dimerization on the conformation of the unliganded complementarity-determining regions (CDR) of a TCR. This structure of an individual Vαmodule has implications for stability and bioengineering of isolated antibody and immunoglobulin domains.