ArticleJournal of structural biology2010
What makes tropomyosin an actin binding protein? A perspective.
Article in Journal of structural biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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Who cites it
22 citing papers in PubMed, 37 citations in OpenAlex.
- Thin filament cardiomyopathies: A review of genetics, disease mechanisms, and emerging therapeutics.Frontiers in cardiovascular medicine · 2022Review
- Mutations Q93H and E97K inInternational journal of molecular sciences · 2021Article
- Impact of A134 and E218 Amino Acid Residues of Tropomyosin on Its Flexibility and Function.International journal of molecular sciences · 2020Article
- Regulation of Actin Filament Length by Muscle Isoforms of Tropomyosin and Cofilin.International journal of molecular sciences · 2020Article
- Thin filament dysfunctions caused by mutations in tropomyosin Tpm3.12 and Tpm1.1.Journal of muscle research and cell motility · 2020Review
- The Effect of Tropomyosin Mutations on Actin-Tropomyosin Binding: In Search of Lost Time.Biophysical journal · 2019Article
- Collagen mimetic peptide discs promote assembly of a broad range of natural protein fibers through hydrophobic interactions.Organic & biomolecular chemistry · 2017Article
- Investigating the effects of tropomyosin mutations on its flexibility and interactions with filamentous actin using molecular dynamics simulation.Journal of muscle research and cell motility · 2016Article
- Mechanistic heterogeneity in contractile properties of α-tropomyosin (TPM1) mutants associated with inherited cardiomyopathies.The Journal of biological chemistry · 2015Article
- The structural dynamics of α-tropomyosin on F-actin shape the overlap complex between adjacent tropomyosin molecules.Archives of biochemistry and biophysics · 2014Article
- Calcium-dependent interaction sites of tropomyosin on reconstituted muscle thin filaments with bound Myosin heads as studied by site-directed spin-labeling.Biophysical journal · 2013Article
- Probing the flexibility of tropomyosin and its binding to filamentous actin using molecular dynamics simulations.Biophysical journal · 2013Article
- Equilibrium self-association of tropomyosin.FEBS letters · 2012Article
- Structural attributes for the recognition of weak and anomalous regions in coiled-coils of myosins and other motor proteins.BMC research notes · 2012Article
- N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Article
- Integrative structural modelling of the cardiac thin filament: energetics at the interface and conservation patterns reveal a spotlight on period 2 of tropomyosin.Bioinformatics and biology insights · 2012Article
- The role of tropomyosin domains in cooperative activation of the actin-myosin interaction.Journal of molecular biology · 2011Article
- Interaction sites of tropomyosin in muscle thin filament as identified by site-directed spin-labeling.Biophysical journal · 2011Article
- Conserved noncanonical residue Gly-126 confers instability to the middle part of the tropomyosin molecule.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Tropomyosin is a two-chained alpha-helical coiled coil that binds along the length of the actin filament and regulates its function. The paper addresses the question of how a "simple" coiled-coil sequence encodes the information for binding and regulating the actin filament, its universal target. Determination of the tropomyosin sequence confirmed Crick's predicted heptapeptide repeat of hydrophobic interface residues and revealed additional features that have been shown to be important for its function: a 7-fold periodicity predicted to correspond to actin binding sites and interruptions of the canonical interface with destabilizing residues, such as Ala. Evidence from published work is summarized, leading to the proposal of a paradigm that binding of tropomyosin to the actin filament requires local instability as well as regions of flexibility. The flexibility derives from bends and local unfolding at regions with a destabilized coiled-coil interface, as well as from the dynamic end-to-end complex. The features are required for tropomyosin to assume the form of the helical actin filament, and to bind to actin monomers along its length. The requirement of instability/flexibility for binding may be generalized to the binding of other coiled coils to their targets.
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Registered trials
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.