8. Conclusion
Three of the four states anticipated by the Lymn-Taylor cross-bridge cycle are now known in atomic detail. The “unbound” states, which are more easily available to protein crystallographic analysis, have yielded most information. The connections between ATP binding and the conformation of the myosin cross-bridge in solution are well understood. Besides being an ATPase the myosin “head” has two essential functions: a shape change induced by product release that drives contraction; a large change of affinity for actin induced by binding ATP. X-ray crystallography, in conjunction with electron microscopy has recently yielded an explanation of both these phenomena in molecular terms. The detailed structures of the actin bound states are gradually becoming available by combining crystal structures analysis with high-resolution electron microscopy. However, the structure of the ephemeral strong binding at the beginning of the power stroke can at present only be inferred.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2005 Springer Science+Business Media, Inc.
About this paper
Cite this paper
Holmes, K.C. (2005). The Molecular Basis of Cross-Bridge Function. In: Sugi, H. (eds) Sliding Filament Mechanism in Muscle Contraction. Advances in Experimental Medicine and Biology, vol 565. Springer, Boston, MA. https://doi.org/10.1007/0-387-24990-7_2
Download citation
DOI: https://doi.org/10.1007/0-387-24990-7_2
Publisher Name: Springer, Boston, MA
Print ISBN: 978-0-387-24989-6
Online ISBN: 978-0-387-24990-2
eBook Packages: MedicineMedicine (R0)