三种ADAMTS13去整合素样结构域突变致蛋白功能缺陷及其与血栓关联的研究

林莉亚, 吴希, 毛胤祺, 陈光明, 武文漫, 戴菁, 王学锋, 丁秋兰

Three disintegrin-like domain mutations of ADAMTS13： functional deficiency and association with thrombosis

LIN Liya, WU Xi, MAO Yinqi, CHEN Guangming, WU Wenman, DAI Jing, WANG Xuefeng, DING Qiulan

图4 ADAMTS13去整合素样结构域的2种氨基酸位点（Pro301、Arg349）及其突变对结构的影响 A：野生型ADAMTS13蛋白质结构，金属蛋白酶结构域上的催化活性中心（HIS-224、GLN-225、HIS-228、HIS-234）和本文研究的突变位点（PRO-301、ARG-349）以红色标出。B：野生型ADAMTS13氨基酸残基PRO-301与突变型ADAMTS13中氨基酸残基ALA-301、ARG-301的结构差异对比。突变后的ARG-301残基周围的红色圆盘表示发生的空间位阻效应。C：野生型ADAMTS13氨基酸残基ARG-349与突变型ADAMTS13中氨基酸残基CYS-349的结构差异对比。

Figure 4 Two amino acid residues (Pro301 and Arg349) in the disintegrin-like domain of ADAMTS13 and the structural effects of their variants A: The structure of wild-type ADAMTS13 protein, with the catalytic active site (HIS-224, GLN-225, HIS-228, HIS-234) in the metalloprotease domain and the studied variant sites (PRO-301, ARG-349) highlighted in red. B: Structural comparison between wild-type ADAMTS13 residue PRO-301 and mutated residues ALA-301 and ARG-301 in ADAMTS13. The red disks surrounding the ARG-301 residue represent steric hindrance caused by the variant. C: Structural comparison between wild-type ADAMTS13 residue ARG-349 and mutated residue CYS-349 in ADAMTS13.