The nature of the actin cross-bridge interaction.
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.
D000199:Actins / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D005426:Flight, Animal; D007313:Insecta; D046911:Macromolecular Substances; D009119:Muscle Contraction; D009132:Muscles / Q000502:physiology*; D015879:Myosin Subfragments; D009218:Myosins / Q000378:metabolism*; D010446:Peptide Fragments / Q000032:analysis / Q000378:metabolism*; D014961:X-Ray Diffraction
D000199:Actins; D046911:Macromolecular Substances; D015879:Myosin Subfragments; D010446:Peptide Fragments; D000255:Adenosine Triphosphate; D009218:Myosins