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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure, crystal packing and molecular dynamics of the calponin-homology domain of Schizosaccharomyces pombe Rng2.
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Structure, crystal packing and molecular dynamics of the calponin-homology domain of Schizosaccharomyces pombe Rng2.

机译：包装结构、晶体和分子动力学calponin-homology域的

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摘要

Schizosaccharomyces pombe Rng2 is an IQGAP protein that is essential for the assembly of an actomyosin ring during cytokinesis. Rng2 contains an amino-terminal calponin-homology (CH) domain, 11 IQ repeats and a RasGAP-homology domain. CH domains are known mainly for their ability to bind F-actin, although they have other ligands in vivo and there are only few examples of actin-binding single CH domains. The structures of several CH domains have already been reported, but this is only the third report of an actin-binding protein that contains a single CH domain (the structures of calponin and EB1 have been reported previously). The 2.21 A resolution crystal structure of the amino-terminal 190 residues of Rng2 from Br- and Hg-derivatives includes 40 residues (150-190) carboxyl-terminal to the CH domain that resemble neither the extended conformation seen in utrophin, nor the compact conformation seen in fimbrin, although residues 154-160 form an unstructured coil which adopts a substructure similar to dystrophin residues 240-246 in the carboxyl-terminal portion of the CH2 domain. This region wraps around the stretch of residues that would be equivalent to the proposed actin-binding site ABS1 and ABS2 from dystrophin. This distinctive feature is absent from previously published CH-domain structures. Another feature revealed by comparing the two derivatives is the presence of two loop conformations between Tyr92 and Arg99.
机译：粟酒裂殖酵母Rng2 IQGAP蛋白质这是基本的组装肌动球蛋白环在胞质分裂。一个伴calponin-homology (CH)领域,11智商重复和RasGAP-homology域。域主要的能力f -肌动蛋白结合,尽管他们有其他的配体体内,只有一些例子actin-binding单一CH域。几个CH域已经被报道,但这只是第三的报告包含一个CH actin-binding蛋白质域(calponin和EB1的结构之前报告)。晶体结构的伴190年残留的Rng2 Br和Hg-derivatives包括40残留物(150 - 190)羧基末端既不像CH域延伸的构象在拉到,也没有紧凑的丝束蛋白构象,虽然残留154 - 160形成一个非结构化的线圈采用类似肌营养不良蛋白的子结构残留在羧基末端部分240 - 246CH2的域。的残留物,相当于拟议中的actin-binding ABS1和ABS2的地点肌营养不良蛋白。缺席CH-domain以前发表的结果结构。这两个衍生品是两个循环的存在构象Tyr92和Arg99之间。

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