ReviewJournal of muscle research and cell motility1989
Functional sequences of the myosin head.
Review in Journal of muscle research and cell motility, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Point mutations in human beta cardiac myosin heavy chain have differential effects on sarcomeric structure and assembly: an ATP binding site change disrupts both thick and thin filaments, whereas hypertrophic cardiomyopathy mutations display normal assembly.The Journal of cell biology · 1997Article
- Telokin (kinase-related protein) modulates the oligomeric state of smooth-muscle myosin light-chain kinase and its interaction with myosin filaments.The Biochemical journal · 1997Article
- Mapping of the actomyosin interfaces.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- Ca(2+)-calmodulin-dependent modification of smooth-muscle myosin light-chain kinase leading to its co-operative activation by calmodulin.The Biochemical journal · 1993Article
- Transient kinetics of the interaction of actin with myosin subfragment-1 in the absence of nucleotide.Biophysical journal · 1993Article
- Identification, characterization and cloning of myr 1, a mammalian myosin-I.The Journal of cell biology · 1993Article
- Localization of myosin heavy chain A in the human pathogen Entamoeba histolytica.Infection and immunity · 1993Article
- Muscle-specific accumulation of Drosophila myosin heavy chains: a splicing mutation in an alternative exon results in an isoform substitution.The EMBO journal · 1991Article
- Molecular charge dominates the inhibition of actomyosin in skinned muscle fibers by SH1 peptides.Biophysical journal · 1991Article
- Effects of sulphydryl modification on skinned rat skeletal muscle fibres using 5,5'-dithiobis(2-nitrobenzoic acid).The Journal of physiology · 1991Article
- The yeast type II myosin heavy chain: analysis of its predicted polypeptide sequence.Journal of muscle research and cell motility · 1991Article
- Expression of human beta-myosin heavy chain fragments in Escherichia coli; localization of actin interfaces on cardiac myosin.Journal of muscle research and cell motility · 1990Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Muscle contraction originates from the sliding of myosin filaments on actin filaments, the energy for which is supplied by the hydrolysis of adenosine-5-triphosphate (ATP) by myosin. The nucleotide first binds to the acto-myosin complex in the myosin head (or subfragment-1), producing a conformational change which induces actin dissociation. The release of phosphate (Pi) then allows a return to the strong actin-myosin association, corresponding to the rigor state. We discuss here certain controversial points arising from current concepts of the actin and nucleotide binding regions at the amino acid sequence level within the subfragment-1 heavy chain. We consider the actin and nucleotide binding regions to be two distinct sites (for each of these regions) one of which is shared competitively between actin and the nucleotide. In our model the cyclical actin-S1 association-dissociation steps correspond to different ATP, actin and ADP affinities for the same amino acid sequence of the S1 heavy chain, contributing alternatively to a single hydrolytic nucleotide site or a strong actin site. We propose the existence of a flexible segment that forms or dismantles the nucleotide or actin sites. The large region (amino acids 540-707) overlapping the actin-myosin interface appears to be the main flexible region of the S1 molecule and we propose that this particular sequence plays a key role in the dissociation pathway of the actin-myosin complex and in the conversion of chemical energy into the mechanical energy of contraction.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.