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Cited by 244

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Deciphering the design of the tropomyosin molecule

Open access
Brown, Jerry H., Kim, Kyoung-Hee, Jun, Gyo, Greenfield, Norma J., Dominguez, Roberto, Volkmann, Niels, Hitchcock-DeGregori, Sarah E., Cohen, Carolyn·2001·Proceedings of the National Academy of Sciences

Abstract

The crystal structure at 2.0-Å resolution of an 81-residue N-terminal fragment of muscle α-tropomyosin reveals a parallel two-stranded α-helical coiled-coil structure with a remarkable core. The high alanine content of the molecule is clustered into short regions where the local 2-fold symmetry is broken by a small (≈1.2-Å) axial staggering of the helices. The joining of these regions with neighboring segments, where the helices are in axial register, gives rise to specific bends in the molecular axis. We observe such bends to be widely distributed in two-stranded α-helical coiled-coil proteins. This asymmetric design in a dimer of identical (or highly similar) sequences allows the tropomyosin molecule to adopt multiple bent conformations. The seven alanine clusters in the core of the complete molecule (which spans seven monomers of the actin helix) promote the semiflexible winding of the tropomyosin filament necessary for its regulatory role in muscle contraction.

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Crossref · 10.1073/pnas.131219198

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Metadata

Authors
Brown, J. H., Kim, K.-H., Jun, G., Greenfield, N. J., Dominguez, R., Volkmann, N., Hitchcock-DeGregori, S. E., & Cohen, C.
Venue
Proceedings of the National Academy of Sciences
Published
2001-07-03
Volume
98
Issue
15
Pages
8496-8501
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2038253226
Cited by
244
References
4
FWCI
4.89
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Deciphering the design of the tropomyosin molecule. https://app.cochat.ai/papers/10.1073/pnas.131219198
The paper
Brown, J. H., Kim, K.-H., Jun, G., Greenfield, N. J., Dominguez, R., Volkmann, N., Hitchcock-DeGregori, S. E., & Cohen, C. (2001). Deciphering the design of the tropomyosin molecule. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.131219198

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.