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Brownian dynamics of interactions between aldolase mutants and F-actin

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

Publisher
John Wiley and Sons
Year
2002
Tongue
English
Weight
387 KB
Volume
15
Category
Article
ISSN
0952-3499

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✦ Synopsis

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‐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.

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