The nature of the actin cross-bridge interaction

Holmes, Kenneth C.; Goody, Roger S.

doi:10.1007/978-1-4684-4703-3_34

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The nature of the actin cross-bridge interaction

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Holmes, Kenneth C.
Protein Cristallography XDS, Max Planck Institute for Medical Research, Max Planck Society;
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Muscle Research, Max Planck Institute for Medical Research, Max Planck Society;

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Goody, Roger S.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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https://link.springer.com/content/pdf/10.1007%2F978-1-4684-4703-3_34.pdf
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引用

Holmes, K. C., & Goody, R. S. (1984). The nature of the actin cross-bridge interaction. Advances in Experimental Medicine and Biology, 170, 374-384. doi:10.1007/978-1-4684-4703-3_34.

引用: https://hdl.handle.net/11858/00-001M-0000-0019-AF9A-D

要旨

Evidence from sequence studies and from proteolysis suggests that S1 consists of three domains Cross-linking studies show that one S1 can bind to two actin monomers which may lie in different strands of the actin long helix. The S1-actin interaction comprises two states “weak” and “strong”. We suggest there are distinct hinged binding sites, “weak” and “rigor”, of which only the rigor site is sensitive to tropomyosin control. If one takes the weak binding domain to be a “nose-cone” which is attached to the rest of the S1 by a flexible covalent hinge allowing the rigor link to be formed independently a number of structural phenomena observed in fibres may be explained.