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首页> 外文期刊>日本结晶学会志 >Crystal Structure Analysis of Human Autocrine Motility Factor
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Crystal Structure Analysis of Human Autocrine Motility Factor

机译：人类自分泌运动因子的晶体结构分析

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Autocrine motility factor (AMF), a tumor-secreted cytokine, stimulates cell migration in vitro and metastasis in viva. AMF is genetically identical to the extracellular cytokines neuroleukin (NLK) and maturation factor (MF) and, interestingly, to the intracellular enzyme phosphoglucose isomerase(PGI). The crystal structures of the inhibitor-free open form and the inhibitor-bound closed form of human AMF have been determined at 1.9 A and 2.4 A resolution, respectively. Upon inhibitor binding, local conformation changes occur around the inhibitor-binding site. The inhibitor-bound structure shows that the location of the inhibitor (of cytokine activity) binding site of human AMF is very similar to those of the inhibitor (of enzymatic activity) binding sites of PGIs. The present study clearly shows that there is structural overlap of the regions responsible for the enzymatic and cytokine functions of AMF/PGI and suggests two scenarios for the inhibition mechanism of cytokine activity of AMF by the carbohydrate phosphate.
机译：自分泌运动因子（AMF）是一种肿瘤分泌的细胞因子，在体外刺激细胞迁移并在体内转移。 AMF在遗传上与细胞外细胞因子神经白蛋白（NLK）和成熟因子（MF）相同，并且与细胞内酶磷酸葡萄糖异构酶（PGI）相同。人AMF的无抑制剂开放形式和抑制剂结合封闭形式的晶体结构已分别以1.9 A和2.4 A的分辨率测定。抑制剂结合后，局部构象变化发生在抑制剂结合位点附近。抑制剂结合的结构表明，人AMF的抑制剂（具有细胞因子活性）结合位点的位置与PGI的抑制剂（具有酶促活性）结合位点的位置非常相似。本研究清楚地表明，负责AMF / PGI的酶和细胞因子功能的区域存在结构重叠，并提出了两种方案来抑制碳水化合物磷酸对AMF的细胞因子活性的作用。

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