Evidence map›Paper›PMID 20465283›Full record

ArticleBiochemistry2010

Structure of the tropomyosin overlap complex from chicken smooth muscle: insight into the diversity of N-terminal recognition.

Jeremiah Frye, Vadim A Klenchin, Ivan Rayment

Abstract readComparative Study
In one paragraph

Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

47 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
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  8. Structural insights into the tropomodulin assembly at the pointed ends of actin filaments.Protein science : a publication of the Protein Society · 2021
    Article
  9. Article
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  11. Review
  12. Actin-tropomyosin distribution in non-muscle cells.Journal of muscle research and cell motility · 2020
    Review
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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

3 authors at 1 institution in 1 country.

Jeremiah FryeDepartment of Biochemistry, University of Wisconsin, Madison, Wisconsin 53706, USA.
Vadim A Klenchin
Ivan Rayment
University of Wisconsin–Madison · US

Funding

Structure Function Studies of the Spindle-Pole Body in Saccharomyces CerevisiaeR01GM083987 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI RAYMENT, IVAN · 2009 to 2012
$1.3M
Structural Studies of Myosin Motor ProteinsR01GM086351 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI RAYMENT, IVAN · 2009 to 2010
$586k
NIGMS NIH HHS GM083987NIGMS NIH HHS GM086351NIGMS NIH HHS R01 GM083987NIGMS NIH HHS R01 GM086351
6 · The paper itself

Abstract

Tropomyosin is a stereotypical alpha-helical coiled coil that polymerizes to form a filamentous macromolecular assembly that lies on the surface of F-actin. The interaction between the C-terminal and N-terminal segments on adjacent molecules is known as the overlap region. We report here two X-ray structures of the chicken smooth muscle tropomyosin overlap complex. A novel approach was used to stabilize the C-terminal and N-terminal fragments. Globular domains from both the human DNA ligase binding protein XRCC4 and bacteriophage varphi29 scaffolding protein Gp7 were fused to 37 and 28 C-terminal amino acid residues of tropomyosin, respectively, whereas the 29 N-terminal amino acids of tropomyosin were fused to the C-terminal helix bundle of microtubule binding protein EB1. The structures of both the XRCC4 and Gp7 fusion proteins complexed with the N-terminal EB1 fusion contain a very similar helix bundle in the overlap region that encompasses approximately 15 residues. The C-terminal coiled coil opens to allow formation of the helix bundle, which is stabilized by hydrophobic interactions. These structures are similar to that observed in the NMR structure of the rat skeletal overlap complex [Greenfield, N. J., et al. (2006) J. Mol. Biol. 364, 80-96]. The interactions between the N- and C-terminal coiled coils of smooth muscle tropomyosin show significant curvature, which differs somewhat between the two structures and implies flexibility in the overlap complex, at least in solution. This is likely an important attribute that allows tropomyosin to assemble around the actin filaments. These structures provide a molecular explanation for the role of N-acetylation in the assembly of native tropomyosin.

Indexed as

Amino Acid SequenceAnimalsAvian ProteinsBacillus PhagesChickensCrystallography, X-RayDNA-Binding ProteinsHumansMacromolecular SubstancesMolecular Sequence DataMuscle ProteinsMuscle, SmoothPeptide FragmentsProtein StabilityProtein Structure, TertiaryRatsAvian ProteinsDNA-Binding ProteinsMacromolecular SubstancesMuscle ProteinsPeptide FragmentsRecombinant Fusion ProteinsTropomyosinXRCC4 protein, human

Identifiers

PMID20465283
PMCPMC2883815
OpenAlexW1965431973

What OpenQuestion holds

Textmetadata
LicenceTDM
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.