Expression, purification and preliminary crystallographic characterization of a novel segment from the neurofibromatosis type 1 protein
Expression, purification and preliminary crystallographic characterization of a novel segment from the neurofibromatosis type 1 protein
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DOI：
10.1107/s0907444904026861
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发表时间：
2004-12-01
影响因子：
2.2
通讯作者：
Scheffzek, K
中科院分区：
文献类型：
--
作者：
Bonneau, F;D'Angelo, I;Scheffzek, K
神经纤维蛋白（MW 320 kDa）是1型神经纤维瘤病（NF1）发病机制的蛋白，NF1是世界上最常见的遗传性疾病之一。神经纤维蛋白gap相关结构域（GRD, MW 38 kDa）具有ras特异性的gtpase激活蛋白特性，这是目前唯一明确的生化功能。本文描述了位于GRD c末端的神经纤维蛋白片段的细菌生产和初步x射线晶体学分析的研究，该片段包含一个据报道与酵母Sec14p脂质交换蛋白同源的区域。在获得的三种晶体变体中，四角形的衍射分辨率至少为2.3埃。
Neurofibromin (MW 320 kDa) is the protein responsible for the pathogenesis of neurofibromatosis type 1 (NF1), one of the most common genetic diseases worldwide. The neurofibromin GAP-related domain (GRD, MW 38 kDa) possess a Ras-specific GTPase-activating protein property, which is at present its only clear biochemical function. This article describes the study of the bacterial production and preliminary X-ray crystallographic analysis of a neurofibromin fragment located at the C-terminal end of the GRD, which contains a region reported to be homologous to the yeast Sec14p lipid exchange protein. Of the three crystal variants obtained, a tetragonal form diffracted to a resolution of at least 2.3 Angstrom.