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Brownian dynamics of interactions between glyceraldehyde-3-phosphate dehydrogenase (GAPDH) mutants and F-actin

✍ Scribed by Victor F. Waingeh; Stephen L. Lowe; Kathryn A. Thomasson

Publisher
Wiley (John Wiley & Sons)
Year
2004
Tongue
English
Weight
316 KB
Volume
73
Category
Article
ISSN
0006-3525

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✦ Synopsis

Abstract

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

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## Abstract 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‐termin