Nucleotide switches in molecular motors: structural analysis of kinesins and myosins.
Recent breakthroughs in the structural biology of cytoskeletal motor proteins show that two distinct families of motors--kinesins and myosins - use a similar mechanism of conformational switching for converting small structural changes in their nucleotide-binding sites into larger movements to provide force generation and motion. This mechanism is found to be similar to that employed by G proteins, the well-known molecular switches that regulate protein-protein interactions in many biological systems.
Sablin
E P
EP
Department of Biochemistry and Biophysics, University of California, 513 Parnassus Avenue, San Francisco, CA 94143, USA.
Fletterick
R J
RJ
D020134:Catalytic Domain; D005544:Forecasting; D016547:Kinesins / Q000502:physiology*; D020409:Molecular Motor Proteins / Q000502:physiology*; D009218:Myosins / Q000502:physiology*; D009711:Nucleotides; D011487:Protein Conformation
D020409:Molecular Motor Proteins; D009711:Nucleotides; D009218:Myosins; D016547:Kinesins