ArticleBiophysical journal2002
A model of cross-bridge attachment to actin in the A*M*ATP state based on x-ray diffraction from permeabilized rabbit psoas muscle.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 33 citations in OpenAlex.
- Structural OFF/ON transitions of myosin in relaxed porcine myocardium predict calcium-activated force.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Small Angle X-ray Diffraction as a Tool for Structural Characterization of Muscle Disease.International journal of molecular sciences · 2022Review
- Septin 9 Exhibits Polymorphic Binding to F-Actin and Inhibits Myosin and Cofilin Activity.Journal of molecular biology · 2015Article
- A novel actin binding site of myosin required for effective muscle contraction.Nature structural & molecular biology · 2012Article
- The N-terminal domains of myosin binding protein C can bind polymorphically to F-actin.Journal of molecular biology · 2011Article
- Electron tomography of cryofixed, isometrically contracting insect flight muscle reveals novel actin-myosin interactions.PloS one · 2010Article
- A mathematical analysis of obstructed diffusion within skeletal muscle.Biophysical journal · 2009Article
- Direct modeling of X-ray diffraction pattern from contracting skeletal muscle.Biophysical journal · 2008Article
- Structural characterization of the binding of Myosin*ADP*Pi to actin in permeabilized rabbit psoas muscle.Biophysical journal · 2006Article
- Initiation of the power stroke in muscle: insights from the phosphate analog AlF4.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Cross-bridge number, position, and angle in target zones of cryofixed isometrically active insect flight muscle.Biophysical journal · 2004Article
- Static and dynamic x-ray diffraction recordings from living mammalian and amphibian skeletal muscles.Biophysical journal · 2003Article
- Structural characterization of weakly attached cross-bridges in the A*M*ATP state in permeabilized rabbit psoas muscle.Biophysical journal · 2002Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
A model of cross-bridges binding to actin in the weak binding A*M*ATP state is presented. The modeling was based on the x-ray diffraction patterns from the relaxed skinned rabbit psoas muscle fibers where ATP hydrolysis was inhibited by N-phenylmaleimide treatment (S. Xu, J. Gu, G. Melvin, L. C. Yu. 2002. Biophys. J. 82:2111-2122). Calculations included both the myosin filaments and the actin filaments of the muscle cells, and the binding to actin was assumed to be single headed. To achieve a good fit, considerable flexibility in the orientation of the myosin head and the position of the S1-S2 junction is necessary, such that the myosin head can bind to a nearby actin whereas the tail end was kept in the proximity of the helical track of the myosin filament. Hence, the best-fit model shows that the head binds to actin in a wide range of orientations, and the tail end deviates substantially from its lattice position in the radial direction (approximately 60 A). Surprisingly, the best fit model reveals that the detached head, whose location thus far has remained undetected, seems to be located close to the surface of the myosin filament. Another significant requirement of the best-fit model is that the binding site on actin is near the N terminus of the actin subunit, a position distinct from the putative rigor-binding site. The results support the idea that the essential role played by the weak binding states M*ATP <--> A*M*ATP for force generation lies in its flexibility, because the probability of attachment is greatly increased, compared with the weak binding M*ADP*P(i) <--> A*M*ADP*P(i) states.
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