Evidence map›Paper›PMID 24854015›Full record

ArticlePLoS computational biology2014

High-resolution modeling of transmembrane helical protein structures from distant homologues.

Kuang-Yui M Chen, Jiaming Sun, Jason S Salvo, David Baker, Patrick Barth

Open access · goldAbstract read
In one paragraph

Article in PLoS computational biology, 2014. 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
2.1field-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

16 citing papers in PubMed, 36 citations in OpenAlex.

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  8. Reprogramming G protein coupled receptor structure and function.Current opinion in structural biology · 2018
    Review
  9. Computational design of orthogonal membrane receptor-effector switches for rewiring signaling pathways.Proceedings of the National Academy of Sciences of the United States of America · 2018
    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

5 authors at 2 institutions in 1 country.

Kuang-Yui M ChenVerna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas, United States of America.
Jiaming SunDepartment of Pharmacology, Baylor College of Medicine, Houston, Texas, United States of America.
Jason S SalvoStructural and Computational Biology and Molecular Biophysics Graduate Program, Baylor College of Medicine, Houston, Texas, United States of America.
David BakerHoward Hughes Medical Institute and Department of Biochemistry, University of Washington, Seattle, Washington, United States of America.
Patrick BarthVerna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas, United States of America; Department of Pharmacology, Baylor College of Medicine, Houston, Texas, United States of America; Structural and Computational Biology and Molecular Biophysics Graduate Program, Baylor College of Medicine, Houston, Texas, United States of America.
Baylor College of Medicine · USHoward Hughes Medical Institute · US

Funding

HOUSTON AREA MOLECULAR BIOPHYSICS TRAINING PROGRAMT32GM008280 · NIGMS · RICE UNIVERSITY · PI WENSEL, THEODORE G · 1988 to 2023
$8.0M
EXPLORING STRUCTURE AND SEQUENCE SPACES OF G PROTEIN-COUPLED RECEPTOR SIGNALINGR01GM097207 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI BARTH, PATRICK DANIEL, WENSEL, THEODORE G · 2012 to 2020
$2.8M
Howard Hughes Medical InstituteNIGMS NIH HHS 1R01GM097207-01A1NIGMS NIH HHS R01 GM097207NIGMS NIH HHS T32 GM008280NIGMS NIH HHS T32GM008280
6 · The paper itself

Abstract

Eukaryotic transmembrane helical (TMH) proteins perform a wide diversity of critical cellular functions, but remain structurally largely uncharacterized and their high-resolution structure prediction is currently hindered by the lack of close structural homologues. To address this problem, we present a novel and generic method for accurately modeling large TMH protein structures from distant homologues exhibiting distinct loop and TMH conformations. Models of the adenosine A2AR and chemokine CXCR4 receptors were first ranked in GPCR-DOCK blind prediction contests in the receptor structure accuracy category. In a benchmark of 50 TMH protein homolog pairs of diverse topology (from 5 to 12 TMHs), size (from 183 to 420 residues) and sequence identity (from 15% to 70%), the method improves most starting templates, and achieves near-atomic accuracy prediction of membrane-embedded regions. Unlike starting templates, the models are of suitable quality for computer-based protein engineering: redesigned models and redesigned X-ray structures exhibit very similar native interactions. The method should prove useful for the atom-level modeling and design of a large fraction of structurally uncharacterized TMH proteins from a wide range of structural homologues.

Indexed as

Models, ChemicalAmino Acid SequenceComputer SimulationMembrane ProteinsMolecular Docking SimulationMolecular Sequence DataProtein ConformationReceptor, Adenosine A2AReceptors, CXCR4Sequence Homology, Amino AcidMembrane ProteinsReceptor, Adenosine A2AReceptors, CXCR4

Identifiers

PMID24854015
PMCPMC4031050
OpenAlexW2020469935

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.