Crystallization and preliminary X-ray analysis of the C-terminal domain of CCM2, part of a novel adaptor protein involved in cerebral cavernous malformations.

Xiaoyan Wang, Jingjin Ding, Dacheng Wang
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Abstract

Cerebral cavernous malformation 2 (CCM2) is a novel two-domain adaptor protein which participates in multiple cellular signalling pathways. Loss-of-function mutations in the gene encoding CCM2 are the cause of common human vascular lesions called cerebral cavernous malformations. Here, the purification, crystallization and preliminary X-ray crystallographic studies of the C-terminal domain of CCM2 (CCM2-Ct) are reported. Diffraction data were collected from native and selenomethionine-substituted crystals of CCM2-Ct to resolutions of 2.9 and 2.7 Å, respectively. Both crystals belonged to space group I4(1)22 with similar unit-cell parameters. The native crystals had unit-cell parameters a = b = 113.29, c = 101.62 Å.

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参与脑海绵畸形的新型适配蛋白 CCM2 的 C 端结构域的结晶和初步 X 射线分析。
脑海绵畸形 2(CCM2)是一种新型双域适配蛋白,参与多种细胞信号通路。编码 CCM2 的基因发生功能缺失突变,是导致称为脑海绵畸形的常见人类血管病变的原因。本文报告了 CCM2 C 端结构域(CCM2-Ct)的纯化、结晶和初步 X 射线晶体学研究。从 CCM2-Ct 的原生晶体和硒代蛋氨酸取代晶体中收集到的衍射数据分辨率分别为 2.9 和 2.7 Å。这两种晶体都属于空间群 I4(1)22,具有相似的单位胞参数。原生晶体的单胞参数为 a = b = 113.29,c = 101.62 Å。
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期刊介绍: Acta Crystallographica Section F is a rapid structural biology communications journal. Articles on any aspect of structural biology, including structures determined using high-throughput methods or from iterative studies such as those used in the pharmaceutical industry, are welcomed by the journal. The journal offers the option of open access, and all communications benefit from unlimited free use of colour illustrations and no page charges. Authors are encouraged to submit multimedia content for publication with their articles. Acta Cryst. F has a dedicated online tool called publBio that is designed to make the preparation and submission of articles easier for authors.
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