Evidence map›Paper›PMID 31155309›Full record

ArticleStructure (London, England : 1993)2019

Structure, Function, and Dynamics of the Gα Binding Domain of Ric-8A.

Baisen Zeng, Tung-Chung Mou, Tzanko I Doukov, Andrea Steiner, Wenxi Yu, Makaia Papasergi-Scott, Gregory G Tall, Franz Hagn, Stephen R Sprang

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
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

16 citing papers in PubMed.

  1. Article
  2. Unisexual reproduction in the global human fungal pathogenProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Unisexual reproduction in the global human fungal pathogenbioRxiv : the preprint server for biology · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Ric-8A, a GEF, and a Chaperone for G Protein α-Subunits: Evidence for the Two-Faced Interface.BioEssays : news and reviews in molecular, cellular and developmental biology · 2020
    Article
  14. Article
  15. Transducin Partners Outside the Phototransduction Pathway.Frontiers in cellular neuroscience · 2020
    Article
  16. 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

9 authors.

Baisen ZengGraduate Program in Biochemistry and Biophysics, University of Montana, Missoula, MT 59812, USA.
Tung-Chung MouCenter for Biomolecular Structure and Dynamics, University of Montana, Missoula, MT 59812, USA; Division of Biological Sciences, University of Montana, Missoula, MT 59812, USA.
Tzanko I DoukovMacromolecular Crystallography Group, Stanford Synchrotron Radiation Light Source, SLAC National Accelerator Laboratory, Stanford University, Stanford, CA 94309, USA.
Andrea SteinerBavarian NMR Center at the Department of Chemistry and Institute for Advanced Study, Technical University of Munich, Ernst-Otto-Fischer-Strasse 2, 85748 Garching, Germany; Institute of Structural Biology, Helmholtz Zentrum München, Ingolstädter Landstrasse 1, 85764 Neuherberg, Germany.
Wenxi YuDepartment of Pharmacology, University of Michigan Medical School, Ann Arbor, MI 48109, USA.
Makaia Papasergi-ScottDepartment of Pharmacology and Physiology, University of Rochester Medical Center, Rochester, NY 14642, USA.
Gregory G TallDepartment of Pharmacology, University of Michigan Medical School, Ann Arbor, MI 48109, USA.
Franz HagnBavarian NMR Center at the Department of Chemistry and Institute for Advanced Study, Technical University of Munich, Ernst-Otto-Fischer-Strasse 2, 85748 Garching, Germany; Institute of Structural Biology, Helmholtz Zentrum München, Ingolstädter Landstrasse 1, 85764 Neuherberg, Germany.
Stephen R SprangGraduate Program in Biochemistry and Biophysics, University of Montana, Missoula, MT 59812, USA; Center for Biomolecular Structure and Dynamics, University of Montana, Missoula, MT 59812, USA; Division of Biological Sciences, University of Montana, Missoula, MT 59812, USA. Electronic address: stephen.sprang@umontana.edu.

Funding

X-ray Scattering Technology CoreP30GM133893 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI Sean McSweeney · 2019 to 2026
$38.6M
X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
Surveillance genome sequencing to detect SARS-CoV-2 virus variants in MontanaP20GM103546 · NIGMS · UNIVERSITY OF MONTANA · PI BOWLER, BRUCE E · 2012 to 2021
$19.2M
Life Science and Biomedical technology Research center at NSLS-II LSBRP41GM111244 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI MCSWEENEY, SEAN · 2014 to 2018
$16.4M
Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
Regulation of Heterotrimeric G proteins by non-receptor activatorsR01GM088242 · NIGMS · UNIVERSITY OF ROCHESTER · PI TALL, GREGORY GORDON · 2009 to 2022
$4.2M
Mechanism of G protein Activation by Ric-8A - competitive revision of R01GM105993R01GM105993 · NIGMS · UNIVERSITY OF MONTANA · PI SPRANG, STEPHEN R · 2013 to 2020
$2.8M
PILATUS3 X 1M X-ray detectorS10OD021512 · OD · STANFORD UNIVERSITY · PI WEIS, WILLIAM I · 2016 to 2016
$550k
NIBIB NIH HHS P30 EB009998NIGMS NIH HHS P20 GM103546NIGMS NIH HHS P30 GM133893NIGMS NIH HHS P41 GM103393NIGMS NIH HHS P41 GM111244NIGMS NIH HHS R01 GM088242NIGMS NIH HHS R01 GM105993NIH HHS S10 OD021512
6 · The paper itself

Abstract

Ric-8A is a 530-amino acid cytoplasmic molecular chaperone and guanine nucleotide exchange factor (GEF) for i, q, and 12/13 classes of heterortrimeric G protein alpha subunits (Gα). We report the 2.2-Å crystal structure of the Ric-8A Gα-binding domain with GEF activity, residues 1-452, and is phosphorylated at Ser435 and Thr440. Residues 1-429 adopt a superhelical fold comprised of Armadillo (ARM) and HEAT repeats, and the C terminus is disordered. One of the phosphorylated residues potentially binds to a basic cluster in an ARM motif. Amino acid sequence conservation and published hydrogen-deuterium exchange data indicate repeats 3 through 6 to be a putative Gα-binding surface. Normal mode modeling of small-angle X-ray scattering data indicates that phosphorylation induces relative rotation between repeats 1-4, 5-6, and 7-9. 2D

Indexed as

Amino Acid SequenceAnimalsBinding SitesCloning, MolecularCrystallography, X-RayEscherichia coliGene ExpressionGenetic VectorsGTP-Binding Protein alpha Subunits, Gi-GoGuanine Nucleotide Exchange FactorsGuanosine TriphosphateHistidineModels, MolecularMutationNuclear ProteinsOligopeptidesGTP-Binding Protein alpha Subunits, Gi-GoGuanine Nucleotide Exchange FactorsGuanosine TriphosphateHis-His-His-His-His-HisHistidineNuclear ProteinsOligopeptidesRecombinant Fusion ProteinsRic8a protein, ratguanine nucleotide exchange factorheteronuclear nuclear magnetic resonanceheterotrimeric G proteinmolecular chaperoneprotein dynamicsprotein structuresmall-angle X-ray scatteringX-ray crystallography

Identifiers

PMID31155309
PMCPMC6610710

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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.