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