Evidence map›Paper›PMID 26043233›Full record

ArticleScientific reports2015

Crystal structure of TRIM20 C-terminal coiled-coil/B30.2 fragment: implications for the recognition of higher order oligomers.

Christopher Weinert, Damien Morger, Aleksandra Djekic, Markus G Grütter, Peer R E Mittl

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing 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

61 citing papers in PubMed, 97 citations in OpenAlex.

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  10. Mechanistic insights from inflammasome structures.Nature reviews. Immunology · 2024
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  12. PML Body Biogenesis: A Delicate Balance of Interactions.International journal of molecular sciences · 2023
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  18. TRIM56 coiled-coil domain structure provides insights into its E3 ligase functions.Computational and structural biotechnology journal · 2023
    Article
  19. Article
  20. Article

1 more citing papers are in PubMed but not listed here.

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

5 authors at 1 institution in 1 country.

Christopher WeinertDepartment of Biochemistry, University Zürich, Winterthurerstrasse 190, 8057 Zürich, Switzerland.
Damien MorgerDepartment of Biochemistry, University Zürich, Winterthurerstrasse 190, 8057 Zürich, Switzerland.
Aleksandra DjekicDepartment of Biochemistry, University Zürich, Winterthurerstrasse 190, 8057 Zürich, Switzerland.
Markus G GrütterDepartment of Biochemistry, University Zürich, Winterthurerstrasse 190, 8057 Zürich, Switzerland.
Peer R E MittlDepartment of Biochemistry, University Zürich, Winterthurerstrasse 190, 8057 Zürich, Switzerland.
University of Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many tripartite motif-containing (TRIM) proteins, comprising RING-finger, B-Box, and coiled-coil domains, carry additional B30.2 domains on the C-terminus of the TRIM motif and are considered to be pattern recognition receptors involved in the detection of higher order oligomers (e.g. viral capsid proteins). To investigate the spatial architecture of domains in TRIM proteins we determined the crystal structure of the TRIM20Δ413 fragment at 2.4 Å resolution. This structure comprises the central helical scaffold (CHS) and C-terminal B30.2 domains and reveals an anti-parallel arrangement of CHS domains placing the B-box domains 170 Å apart from each other. Small-angle X-ray scattering confirmed that the linker between CHS and B30.2 domains is flexible in solution. The crystal structure suggests an interaction between the B30.2 domain and an extended stretch in the CHS domain, which involves residues that are mutated in the inherited disease Familial Mediterranean Fever. Dimerization of B30.2 domains by means of the CHS domain is crucial for TRIM20 to bind pro-IL-1β in vitro. To exemplify how TRIM proteins could be involved in binding higher order oligomers we discuss three possible models for the TRIM5α/HIV-1 capsid interaction assuming different conformations of B30.2 domains.

Indexed as

Models, MolecularProtein Interaction Domains and MotifsCapsidCytoskeletal ProteinsHIV-1HumansInterleukin-1betaProtein BindingProtein ConformationProtein MultimerizationPyrinSolutionsCytoskeletal ProteinsInterleukin-1betaMEFV protein, humanPyrinSolutions

Identifiers

PMID26043233
PMCPMC4455283
OpenAlexW2249738812

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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.