TY - JOUR
T1 - Variable surface loops and myosin activity
T2 - Accessories to a motor
AU - Murphy, C. T.
AU - Spudich, J. A.
N1 - Funding Information:
*To whom correspondence should be addressed: SUMC, Stanford, CA 94305, USA. Tel.: +1 650 7237634; Fax: +1 650 7256044 E-mail: [email protected] This work was supported by NIH Grant 33289 to J.A.S. C.T.M. is a Howard Hughes Medical Institute Predoctoral Fellow.
PY - 2000
Y1 - 2000
N2 - The catalytic head of myosin is a globular structure that has historically been divided into three segments of 25, 50, and 20 kDa. The solvent-exposed, proteolytically-sensitive surface loops of myosin that join these three segments are highly variable in their sequences. While surface loops have not traditionally been thought to affect enzymatic activities, these loops lie near the ATP and actin-binding sites and have been implicated in the modulation of myosin's kinetic activities. In this work we review the wealth of data regarding the loops that has accumulated over the years and discuss the roles of the loops in contributing to the different activities displayed by different myosin isoforms.
AB - The catalytic head of myosin is a globular structure that has historically been divided into three segments of 25, 50, and 20 kDa. The solvent-exposed, proteolytically-sensitive surface loops of myosin that join these three segments are highly variable in their sequences. While surface loops have not traditionally been thought to affect enzymatic activities, these loops lie near the ATP and actin-binding sites and have been implicated in the modulation of myosin's kinetic activities. In this work we review the wealth of data regarding the loops that has accumulated over the years and discuss the roles of the loops in contributing to the different activities displayed by different myosin isoforms.
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U2 - 10.1023/A:1005610007209
DO - 10.1023/A:1005610007209
M3 - Article
C2 - 10961838
AN - SCOPUS:0033866540
SN - 0142-4319
VL - 21
SP - 139
EP - 151
JO - Journal of Muscle Research and Cell Motility
JF - Journal of Muscle Research and Cell Motility
IS - 2
ER -