Brownian dynamics of interactions between aldolase mutants and F-actin.
Brownian dynamics of interactions between aldolase mutants and F-actin.
复制标题
醛缩酶突变体和 F-肌动蛋白之间相互作用的布朗动力学。
DOI：
10.1002/jmr.599
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发表时间：
2002
期刊：
影响因子：
--
通讯作者：
Thomasson,KathrynA
中科院分区：
文献类型：
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作者：
Lowe,StephenL;Atkinson,DerekM;Waingeh,VictorF;Thomasson,KathrynA
以前的布朗动力学（BD）模拟(Ouporov IG， Knull HR和Thomasson KA 1999.生物物理学。[j] . 76: 17-27]研究了醛缩酶与F -肌动蛋白复合物形成过程中的三个赖氨酸残基（K288， K293和K341）和肌动蛋白N端酸性残基（DEDE）。用丙氨酸取代任何赖氨酸残基的醛缩酶突变体的计算机模型的BD模拟显示结合能降低；单个替代的最大影响是K341A，替换所有三种赖氨酸大大降低了结合。野生型兔醛缩酶与改变后的F -肌动蛋白的BD模拟表明，如果4个N端酸性残基中的任何一个被丙氨酸取代，结合能力降低，如果3个或更多的N端酸性残基被取代，结合能力大大降低；这四种肌动蛋白残基中没有一种比其他的对结合更重要。版权所有©2002约翰威利父子有限公司
Previous Brownian dynamics (BD) simulations (Ouporov IG, Knull HR and Thomasson KA 1999.Biophys. J. 76: 17–27) of complex formation between rabbit aldolase and F‐actin have identified three lysine residues (K288, K293 and K341) on aldolase and acidic residues (DEDE) at the N‐terminus of actin as important to binding. BD simulations of computer models of aldolase mutants with any of these lysine residues replaced by alanine show reduced binding energy; the greatest effect of a single substitution is for K341A, and replacement of all three lysines greatly reduces binding. BD simulations of wild‐type rabbit aldolase vs altered F‐actin show that binding is decreased if any one of the four N‐terminal acidic residues is replaced by alanine and binding is greatly reduced if three or more of the N‐terminal acidic residues are replaced; none of the four actin residues appear more critical for binding than the others. Copyright © 2002 John Wiley & Sons, Ltd.