Gorga J C, Brown J H, Jardetzky T, Wiley D C, Strominger J L
Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, MA 02138.
Res Immunol. 1991 Jun-Aug;142(5-6):401-7. doi: 10.1016/0923-2494(91)90038-k.
The class II major histocompatibility antigens HLA-DR1, DR2, DR3, DR4, DR7 and DR8 were purified by immunoaffinity chromatography from homozygous human B lymphoblastoid cell lines. The purified, detergent-soluble molecules were cleaved with the protease papain to remove the hydrophobic transmembrane regions and cytoplasmic tails. Crystals were obtained for each of the papain-solubilized fragments. DR1 crystallized under a variety of different conditions, resulting in two different orthorhombic crystal forms, one of which diffracts as far as 3.5A. Crystals of DR2, DR3, DR4 and DR8 have the same unit cell dimensions as the DR1 crystals, and crystals of DR3 and DR4 have the same diffracting power as the DR1 crystals. The best DR7 crystals obtained thus far are hexagonal and diffract to only about 8A. Crystals of similar hexagonal form have also been observed for most of the other DR subsets.
通过免疫亲和层析从纯合的人B淋巴母细胞系中纯化出II类主要组织相容性抗原HLA - DR1、DR2、DR3、DR4、DR7和DR8。用蛋白酶木瓜蛋白酶切割纯化的、可溶于去污剂的分子，以去除疏水跨膜区和细胞质尾巴。获得了每种木瓜蛋白酶溶解片段的晶体。DR1在多种不同条件下结晶，形成两种不同的正交晶型，其中一种衍射分辨率可达3.5埃。DR2、DR3、DR4和DR8的晶体与DR1晶体具有相同的晶胞尺寸，DR3和DR4的晶体与DR1晶体具有相同的衍射能力。迄今为止获得的最佳DR7晶体为六方晶型，衍射分辨率仅约为8埃。在大多数其他DR亚组中也观察到了类似的六方晶型晶体。
