Evidence map›Paper›PMID 21685921›Full record

ArticleNature structural & molecular biology2011

Integrating energy calculations with functional assays to decipher the specificity of G protein-RGS protein interactions.

Mickey Kosloff, Amanda M Travis, Dustin E Bosch, David P Siderovski, Vadim Y Arshavsky

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2011. 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
2.0field-weighted citation impact, top 13% 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, 54 citations in OpenAlex.

  1. Article
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  4. GαThe FEBS journal · 2025
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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

5 authors at 2 institutions in 1 country.

Mickey KosloffDuke Eye Center, Duke University Medical Center, Durham, North Carolina, USA.
Amanda M Travis
Dustin E Bosch
David P Siderovski
Vadim Y Arshavsky
Duke Medical Center · USUniversity of North Carolina at Chapel Hill · US

Funding

VISION RESEARCHP30EY005722 · NEI · DUKE UNIVERSITY · PI Vadim Y Arshavsky · 1985 to 2026
$19.3M
Molecular mechanisms of photoreceptor outer segment morphogenesisR01EY012859 · NEI · MASSACHUSETTS EYE AND EAR INFIRMARY · PI ARSHAVSKY, VADIM Y · 2000 to 2022
$10.0M
Structural Determinants of Heterotrimeric G-protein Nucleotide CyclingR01GM082892 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI SIDEROVSKI, DAVID P. · 2008 to 2011
$924k
NEI NIH HHS EY012859NEI NIH HHS EY5722NEI NIH HHS P30 EY005722NEI NIH HHS R01 EY012859NIGMS NIH HHS GM082892NIGMS NIH HHS R01 GM082892
6 · The paper itself

Abstract

The diverse Regulator of G protein Signaling (RGS) family sets the timing of G protein signaling. To understand how the structure of RGS proteins determines their common ability to inactivate G proteins and their selective G protein recognition, we combined structure-based energy calculations with biochemical measurements of RGS activity. We found a previously unidentified group of variable 'Modulatory' residues that reside at the periphery of the RGS domain-G protein interface and fine-tune G protein recognition. Mutations of Modulatory residues in high-activity RGS proteins impaired RGS function, whereas redesign of low-activity RGS proteins in critical Modulatory positions yielded complete gain of function. Therefore, RGS proteins combine a conserved core interface with peripheral Modulatory residues to selectively optimize G protein recognition and inactivation. Finally, we show that our approach can be extended to analyze interaction specificity across other large protein families.

Indexed as

Amino Acid SequenceBinding SitesColicinsGTP-Binding ProteinsHumansMolecular Sequence DataMutagenesis, Site-DirectedProtein Interaction Domains and MotifsProtein Interaction MappingProtein Structure, TertiaryRGS ProteinsSequence AlignmentStructure-Activity RelationshipSubstrate SpecificityColicinsGTP-Binding ProteinsRGS Proteins

Identifiers

PMID21685921
PMCPMC3130846
OpenAlexW2139605516

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.