Evidence map›Paper›PMID 25982113›Full record

ArticleMolecular cell2015

Structural Basis for Receptor Activity-Modifying Protein-Dependent Selective Peptide Recognition by a G Protein-Coupled Receptor.

Jason M Booe, Christopher S Walker, James Barwell, Gabriel Kuteyi, John Simms, Muhammad A Jamaluddin, Margaret L Warner, Roslyn M Bill, Paul W Harris, Margaret A Brimble and 3 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
7.5field-weighted citation impact, top 2% 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

60 citing papers in PubMed, 123 citations in OpenAlex.

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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

13 authors at 4 institutions in 3 countries.

Jason M BooeDepartment of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA.
Christopher S WalkerSchool of Biological Sciences and Maurice Wilkins Centre, University of Auckland, Auckland 1142, New Zealand.
James BarwellSchool of Life and Health Sciences, Aston University, Birmingham, B4 7ET, UK.
Gabriel KuteyiSchool of Life and Health Sciences, Aston University, Birmingham, B4 7ET, UK.
John SimmsSchool of Life and Health Sciences, Aston University, Birmingham, B4 7ET, UK.
Muhammad A JamaluddinSchool of Biological Sciences and Maurice Wilkins Centre, University of Auckland, Auckland 1142, New Zealand.
Margaret L WarnerDepartment of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA.
Roslyn M BillSchool of Life and Health Sciences, Aston University, Birmingham, B4 7ET, UK.
Paul W HarrisSchool of Chemical Sciences and Maurice Wilkins Centre, University of Auckland, Auckland 1142, New Zealand.
Margaret A BrimbleSchool of Chemical Sciences and Maurice Wilkins Centre, University of Auckland, Auckland 1142, New Zealand.
David R PoynerSchool of Life and Health Sciences, Aston University, Birmingham, B4 7ET, UK.
Debbie L HaySchool of Biological Sciences and Maurice Wilkins Centre, University of Auckland, Auckland 1142, New Zealand.
Augen A PioszakDepartment of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA. Electronic address: augen-pioszak@ouhsc.edu.
Aston University · GBUniversity of Auckland · NZUniversity of Oklahoma Health Sciences Center · USMaurice Wilkins Centre · NZ

Funding

Structure-Function Studies of MsvR, a Methanogen-Specific Transcriptional RegulaP20GM103640 · NIGMS · UNIVERSITY OF OKLAHOMA · PI MOOERS, BLAINE H. M. · 2012 to 2021
$20.4M
RAMP-altered Class B GPCR Hormone RecognitionR01GM104251 · NIGMS · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI PIOSZAK, AUGEN A · 2012 to 2024
$4.2M
NIGMS NIH HHS P20 GM103640NIGMS NIH HHS P20GM103640NIGMS NIH HHS R01 GM104251NIGMS NIH HHS R01GM104251Wellcome Trust 091496
6 · The paper itself

Abstract

Association of receptor activity-modifying proteins (RAMP1-3) with the G protein-coupled receptor (GPCR) calcitonin receptor-like receptor (CLR) enables selective recognition of the peptides calcitonin gene-related peptide (CGRP) and adrenomedullin (AM) that have diverse functions in the cardiovascular and lymphatic systems. How peptides selectively bind GPCR:RAMP complexes is unknown. We report crystal structures of CGRP analog-bound CLR:RAMP1 and AM-bound CLR:RAMP2 extracellular domain heterodimers at 2.5 and 1.8 Å resolutions, respectively. The peptides similarly occupy a shared binding site on CLR with conformations characterized by a β-turn structure near their C termini rather than the α-helical structure common to peptides that bind related GPCRs. The RAMPs augment the binding site with distinct contacts to the variable C-terminal peptide residues and elicit subtly different CLR conformations. The structures and accompanying pharmacology data reveal how a class of accessory membrane proteins modulate ligand binding of a GPCR and may inform drug development targeting CLR:RAMP complexes.

Indexed as

AdrenomedullinAmino Acid SequenceAnimalsBinding SitesCalcitonin Gene-Related PeptideCalcitonin Receptor-Like ProteinChlorocebus aethiopsCOS CellsCrystallography, X-RayHumansModels, MolecularMolecular Sequence DataMutationPeptidesProtein BindingProtein MultimerizationAdrenomedullinCalcitonin Gene-Related PeptideCalcitonin Receptor-Like ProteinPeptidesRAMP1 protein, humanRAMP2 protein, humanReceptor Activity-Modifying Protein 1Receptor Activity-Modifying Protein 2

Identifiers

PMID25982113
PMCPMC4504005
OpenAlexW1524399027

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.