Evidence map›Paper›PMID 12032291›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2002

The crystal structure of the C-terminal fragment of striated-muscle alpha-tropomyosin reveals a key troponin T recognition site.

Yu Li, Suet Mui, Jerry H Brown, James Strand, Ludmilla Reshetnikova, Larry S Tobacman, Carolyn Cohen

Abstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
3.7field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

45 citing papers in PubMed, 87 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Mechanism of the calcium-regulation of muscle contraction--in pursuit of its structural basis.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2015
    Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Yu LiRosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02454-9110, USA.
Suet Mui
Jerry H Brown
James Strand
Ludmilla Reshetnikova
Larry S Tobacman
Carolyn Cohen
Brandeis University · USUniversity of Iowa · US

Funding

MUSCLE STRUCTURE AND THE CONTRACTILE MECHANISMR01AR017346 · NIAMS · BRANDEIS UNIVERSITY · PI COHEN, CAROLYN · 1986 to 2012
$7.6M
CARDIAC CONTRACTILE PROTEIN COOPERATIVITYR01HL038834 · NHLBI · UNIVERSITY OF IOWA · PI TOBACMAN, LARRY S · 1992 to 2009
$3.6M
CARDIAC CONTRACTILE PROTEIN COOPERATIVITYR29HL038834 · NHLBI · UNIVERSITY OF IOWA · PI TOBACMAN, LARRY S · 1987 to 1991
–
MUSCLE STRUCTURE AND THE CONTRACTILE MECHANISMR37AR017346 · NIAMS · BRANDEIS UNIVERSITY · PI COHEN, CAROLYN · 1990 to 1999
–
NHLBI NIH HHS HL-38834NHLBI NIH HHS R01 HL038834NIAMS NIH HHS AR17346NIAMS NIH HHS R01 AR017346NIAMS NIH HHS R37 AR017346
6 · The paper itself

Abstract

Contraction in striated and cardiac muscles is regulated by the motions of a Ca(2+)-sensitive tropomyosin/troponin switch. In contrast, troponin is absent in other muscle types and in nonmuscle cells, and actomyosin regulation is myosin-linked. Here we report an unusual crystal structure at 2.7 A of the C-terminal 31 residues of rat striated-muscle alpha-tropomyosin (preceded by a fragment of the GCN4 leucine zipper). The C-terminal 22 residues (263-284) of the structure do not form a two-stranded alpha-helical coiled coil as does the rest of the molecule, but here the alpha-helices splay apart and are stabilized by the formation of a tail-to-tail dimer with a symmetry-related molecule. The site of splaying involves a small group of destabilizing core residues that is present only in striated muscle tropomyosin isoforms. These results reveal a specific recognition site for troponin T and clarify the physical basis for the unique regulatory mechanism of striated muscles.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCrystallography, X-RayModels, MolecularMolecular Sequence DataMuscle, SkeletalMutagenesis, Site-DirectedPeptide FragmentsPolymerase Chain ReactionProtein ConformationProtein IsoformsProtein Structure, SecondaryRecombinant ProteinsTropomyosinTroponin TPeptide FragmentsProtein IsoformsRecombinant ProteinsTropomyosinTroponin T

Identifiers

PMID12032291
PMCPMC124239
OpenAlexW1982519867

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.