Evidence map›Paper›PMID 28434917›Full record

ArticleStructure (London, England : 1993)2017

Conformational Dynamics and Allostery in E2:E3 Interactions Drive Ubiquitination: gp78 and Ube2g2.

Kalyan S Chakrabarti, Jess Li, Ranabir Das, R Andrew Byrd

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

18 citing papers in PubMed, 30 citations in OpenAlex.

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  13. Could confounding the allosteric communication of biotic machinery be an alternative path to antibiotics?Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  14. Protein Dynamics revealed by NMR Relaxation Methods.Emerging topics in life sciences · 2020
    Article
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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

4 authors at 3 institutions in 2 countries.

Kalyan S ChakrabartiStructural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, MD 21702-1201, USA.
Jess LiStructural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, MD 21702-1201, USA.
Ranabir DasStructural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, MD 21702-1201, USA; National Center for Biological Sciences, Tata Institute of Fundamental Research, Bangalore 560065, India. Electronic address: rana@ncbs.res.in.
R Andrew ByrdStructural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, MD 21702-1201, USA. Electronic address: byrdra@mail.nih.gov.
National Cancer Institute · USCenter for Cancer Research · USTata Institute of Fundamental Research · IN

Funding

Investigation of Protein-Protein Interactions in the ERAD Ubiquitylation PathwayZIABC011131 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI BYRD, ROBERT · 2009 to 2024
$12.0M
Structural Biology of Proteins Involved in Signal Transduction and Regulation ofZ01BC010346 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI BYRD, R ANDREW · 2000 to 2008
$1.7M
Intramural NIH HHS Z01 BC010346
6 · The paper itself

Abstract

Conformational dynamics plays a fundamental role in molecular recognition and activity in enzymes. The ubiquitin-conjugating enzyme (E2) Ube2g2 functions with the ubiquitin ligase (E3) gp78 to assemble poly-ubiquitin chains on target substrates. Two domains in gp78, RING and G2BR, bind to two distant regions of Ube2g2, and activate it for ubiquitin (Ub) transfer. G2BR increases the affinity between the RING and Ube2g2 by 50-fold, while the RING catalyzes the transfer of Ub from the Ube2g2∼Ub conjugate. How G2BR and RING activate Ube2g2 is unclear. In this work, conformational dynamics in Ube2g2 revealed a clear correlation of binding G2BR and RING with the sequential progression toward Ub transfer. The interrelationship of the existence and exchange between ground and excited states leads to a dynamic energy landscape model, in which redistribution of populations contributes to allostery and activation. These findings provide insight into gp78's modulation of conformational exchange in Ube2g2 to stimulate ubiquitination.

Indexed as

Allosteric SiteUbiquitinationAllosteric RegulationHumansMolecular Dynamics SimulationReceptors, Autocrine Motility FactorUbiquitin-Conjugating EnzymesAMFR protein, humanReceptors, Autocrine Motility FactorUBE2G2 protein, humanUbiquitin-Conjugating EnzymesallosteryCPMG dynamicsdynamic allosteryenergy landscapegp78Ube2g2ubiquitin-conjugating enzymeubiquitin ligase

Identifiers

PMID28434917
PMCPMC5512444
OpenAlexW2605836025

What OpenQuestion holds

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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.