Crystal structure of the MHC class I homolog MIC-A, a γδ T cell ligand
Crystal structure of the MHC class I homolog MIC-A, a γδ T cell ligand
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DOI：
10.1016/s1074-7613(00)80057-6
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发表时间：
1999-05-01
期刊：
影响因子：
32.4
通讯作者：
Strong, RK
中科院分区：
文献类型：
--
作者：
Li, PW;Willie, ST;Strong, RK
主要组织相容性复合体（MHC）I类同源物MIC-A作为应激诱导抗原发挥功能，其被γ δ T细胞亚群识别，不依赖于β 2-微球蛋白和结合肽。它的晶体结构揭示了一个显着改变的MHC I类折叠，无论是在细节和整体结构域组织。肽结合沟的唯一残余物是一个小空腔，该空腔是由于使一个限定沟的螺旋的大部分无序而形成的。β 2-微球蛋白结合的丧失是由于相互作用界面的重组。序列变异的结构图表明，在平台的下侧，在MHC I类-肽复合物上的α β T细胞受体识别的表面的相对侧上，存在潜在的受体结合位点。
The major histocompatibility complex (MHC) class I homolog MIC-A functions as a stress-inducible antigen that is recognized by a subset of gamma delta T cells independent of beta(2)-microglobulin and bound peptides. Its crystal structure reveals a dramatically altered MHC class I fold, both in detail and overall domain organization. The only remnant of a peptide-binding groove is a small cavity formed as the result of disordering a large section of one of the groove-defining helices. Loss of beta(2)-microglobulin binding is due to a restructuring of the interaction interfaces. Structural mapping of sequence variation suggests potential receptor binding sites on the underside of the platform on the side opposite of the surface recognized by alpha beta T cell receptors on MHC class I-peptide complexes.