Brownian dynamics of interactions between glyceraldehyde-3-phosphate dehydrogenase (GAPDH) mutants and F-actin.
Brownian dynamics of interactions between glyceraldehyde-3-phosphate dehydrogenase (GAPDH) mutants and F-actin.
复制标题
3-磷酸甘油醛脱氢酶 (GAPDH) 突变体和 F-肌动蛋白之间相互作用的布朗动力学。
DOI：
10.1002/bip.10560
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发表时间：
2004
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：
Waingeh,VictorF;Lowe,StephenL;Thomasson,KathrynA
对GAPDH突变体与F-肌动蛋白相互作用的计算机模型的布朗动力学模拟强调了这种相互作用的静电性质，并证实了以前在GAPDH结构上发现的四个赖氨酸残基(Ouporov，I.V.；Knul，H.R.；Lowe，S.L.；Thomasson，K.A.JMol Recognit 2001，14，29-41)在这些相互作用中的重要性。突变体是GAPDH模型，在该模型中，一个或多个先前确定的赖氨酸被丙氨酸取代。模拟结果显示，与野生型GAPDH相比，这些突变体与F-肌动蛋白的结合减少。4种赖氨酸的结合作用显著降低，其比静电相互作用能为−7.3±1.0，而野生酶为−11.4±0.5kcal/m ol。BD模拟也重申了四级结构对GAPDH结合F-肌动蛋白的重要性。©2004威利期刊公司，生物聚合物，2004
Brownian dynamics simulations of computer models of GAPDH mutants interacting with F‐actin emphasized the electrostatic nature of such interactions, and confirmed the importance of four previously identified lysine residues on the GAPDH structure (Ouporov, I.V.; Knull, H.R.; Lowe, S.L.; Thomasson, K.A. J Mol Recognit 2001, 14, 29–41) in these interactions. Mutants were GAPDH models in which one or more of the previously identified lysines had been replaced with alanine. Simulations showed reduced binding of these mutants to F‐actin compared to wild‐type GAPDH. Binding was significantly reduced by mutating the four lysines; the specific electrostatic interaction energy of the quadruple mutant was −7.3 ± 1.0 compared to −11.4 ± 0.5 kcal/mol for the wild enzyme. The BD simulations also reaffirmed the importance of quaternary structure for GAPDH binding F‐actin. © 2004 Wiley Periodicals, Inc. Biopolymers, 2004