title: Brownian dynamics of interactions between aldolase mutants and F-actin.
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.
authors.affiliation: Department of Chemistry, University of North Dakota, Grand Forks, ND 58202, USA.
authors.forename: Stephen L
authors.initials: SL
authors.lastname: Lowe
authors.forename: Derek M
authors.initials: DM
authors.lastname: Atkinson
authors.forename: Victor F
authors.initials: VF
authors.lastname: Waingeh
authors.forename: Kathryn A
authors.initials: KA
authors.lastname: Thomasson
mesh_terms: D000199:Actins / Q000378:metabolism*; D000818:Animals; D005634:Fructose-Bisphosphate Aldolase / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D011817:Rabbits
chemical_list: D000199:Actins; D005634:Fructose-Bisphosphate Aldolase