棘阿米巴肌动蛋白结合蛋白-I的三维溶液结构
Three-dimensional solution structure of Acanthamoeba profilin-I.
作者信息
Vinson V K, Archer S J, Lattman E E, Pollard T D, Torchia D A
机构信息
Department of Cell Biology and Anatomy, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
出版信息
J Cell Biol. 1993 Sep;122(6):1277-83. doi: 10.1083/jcb.122.6.1277.
Abstract
We have determined a medium resolution three-dimensional solution structure of Acanthamoeba profilin-I by multidimensional nuclear magnetic resonance spectroscopy. This 13-kD actin binding protein consists of a five stranded antiparallel beta sheet flanked by NH2- and COOH-terminal helices on one face and by a third helix and a two stranded beta sheet on the other face. Data from actin-profilin cross-linking experiments and the localization of conserved residues between profilins in different phyla indicate that actin binding occurs on the molecular face occupied by the terminal helices. The other face of the molecule contains the residues that differ between Acanthamoeba profilins-I and II and may be important in determining the difference in polyphosphoinositide binding between these isoforms. This suggests that lipids and actin bind to different faces of the molecule.
摘要
我们通过多维核磁共振光谱法确定了棘阿米巴肌动蛋白结合蛋白-I的中等分辨率三维溶液结构。这种13-kD的肌动蛋白结合蛋白由一个五链反平行β折叠组成，其一侧由NH2-和COOH-末端螺旋环绕，另一侧由第三个螺旋和一个双链β折叠环绕。肌动蛋白-肌动蛋白结合蛋白交联实验的数据以及不同门中肌动蛋白结合蛋白之间保守残基的定位表明，肌动蛋白结合发生在由末端螺旋占据的分子面上。分子的另一面包含棘阿米巴肌动蛋白结合蛋白-I和II之间不同的残基，可能在决定这些同工型之间多磷酸肌醇结合的差异方面很重要。这表明脂质和肌动蛋白结合到分子的不同面上。
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