Production, crystallization, and preliminary x-ray analysis of the human MHC class Ib molecule HLA-E
Production, crystallization, and preliminary x-ray analysis of the human MHC class Ib molecule HLA-E
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DOI：
10.1002/pro.5560070525
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发表时间：
1998-05-01
期刊：
影响因子：
8
通讯作者：
Jones, EY
中科院分区：
文献类型：
--
作者：
O'Callaghan, CA;Tormo, J;Jones, EY
HLA-E是第一个被结晶的人类Ib类主要组织相容性复合物分子。HLA-E是高度保守的，几乎是非多态性的，最近已被证明是第一个专门的配体的自然杀伤细胞受体。在功能研究中，HLA-E与Ia类MHC分子不同，具有严格限制的肽结合特异性。HLA-E结合一组有限的几乎相同的前导序列肽，这些前导序列肽来源于Ia类分子，并将它们呈递到细胞表面，以供自然杀伤细胞受体识别。我们现在表明，HLA-E的细胞外区域与β 2微球蛋白形成稳定的复合物，并且可以在合成肽周围重折叠。在硫酸铵的存在下，这种复合物的晶体在四到六个月内缓慢形成。晶体的晶胞参数为：a = 182.2埃，B = 182.2埃，c = 88.4埃，空间群为P3（1）21。
HLA-E is the first human class Ib major histocompatibility complex molecule to be crystallized. HLA-E is highly conserved and almost nonpolymorphic, and has recently been shown to be the first specialized ligand for natural killer cell receptors. In functional studies, HLA-E is unlike the class Ia MHC molecules in having tightly restricted peptide binding specificity. HLA-E binds a limited set of almost identical leader sequence peptides derived from class Ia molecules and presents these at the cell surface for recognition by natural killer cell receptors. We now show that the extracellular region of HLA-E forms a stable complex with beta 2 microglobulin and can be refolded around synthetic peptide. Crystals of this complex formed slowly over four to six months in the presence of ammonium sulphate. The crystals diffract to 2.85 A with space group P3(1)21 and unit cell dimensions a = 182.2 Angstrom, b = 182.2 Angstrom, c = 88.4 Angstrom.