Molecular structure of F-actin and location of surface binding sites.
Comparisons of three-dimensional maps of vertebrate muscle thin filaments obtained by cryo-electron microscopy and image analysis, reveal the molecular structure of F-actin, the location of the C terminus of the monomer and the positions of the binding sites of tropomyosin, the myosin head and the N-terminal portion of the myosin A1 light chain on the filament. These data provide strong constraints for evaluating models built from the atomic structure of the monomer and the subsequent identification of molecular contacts.
Milligan
R A
RA
Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, California 92037.
Whittaker
M
M
Safer
D
D
D000199:Actins / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D000818:Animals; D001665:Binding Sites; D007091:Image Processing, Computer-Assisted; D008854:Microscopy, Electron; D015394:Molecular Structure; D009132:Muscles / Q000737:chemistry; D015879:Myosin Subfragments / Q000378:metabolism; D011817:Rabbits; D014335:Tropomyosin / Q000378:metabolism
D000199:Actins; D015879:Myosin Subfragments; D014335:Tropomyosin