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首页> 外文期刊>Acta crystallographica. Section D, Biological crystallography. >Structure of mouse muskelin discoidin domain and biochemical characterization of its self-association
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Structure of mouse muskelin discoidin domain and biochemical characterization of its self-association

机译：鼠标结构muskelin discoidin域和的生化特性self-association

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摘要

Muskelin is an intracellular kelch-repeat protein comprised of discoidin, LisH, CTLH and kelch-repeat domains. It is involved in cell adhesion and the regulation of cytoskeleton dynamics as well as being a component of a putative E3 ligase complex. Here, the first crystal structure of mouse muskelin discoidin domain (MK-DD) is reported at 1.55 angstrom resolution, which reveals a distorted eight-stranded beta-barrel with two short alpha-helices at one end of the barrel. Interestingly, the Nand C-termini are not linked by the disulfide bonds found in other eukaryotic discoidin structures. A highly conserved MIND motif appears to be the determinant for MK-DD specific interaction together with the spike loops. Analysis of interdomain interaction shows that MK-DD binds the kelch-repeat domain directly and that this interaction depends on the presence of the LisH domain.
机译：Muskelin是一种胞内kelch-repeat蛋白质由discoidin、丽斯,CTLH和kelch-repeat域。粘附和细胞骨架的规定动力学以及作为一个组成部分假定的E3连接酶复杂。晶体结构的鼠标muskelin discoidin域(MK-DD)据报道为1.55埃揭示了一个扭曲的决议eight-stranded beta-barrel有两个短阿尔法螺旋筒的一端。有趣的是,与非c终端不联系其他真核生物中的二硫键discoidin结构。主题似乎MK-DD的行列式具体的交互一起飙升循环。直接,MK-DD结合kelch-repeat域互动,这取决于存在丽斯的域。

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