Evidence map›Paper›PMID 17360332›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2007

Structure of the N-terminal domain of a type B1 G protein-coupled receptor in complex with a peptide ligand.

Christy Rani R Grace, Marilyn H Perrin, Jozsef Gulyas, Michael R Digruccio, Jeffrey P Cantle, Jean E Rivier, Wylie W Vale, Roland Riek

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. 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
5.8field-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, 130 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Conformations of peptoids in nanosheets result from the interplay of backbone energetics and intermolecular interactions.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  8. Article
  9. Observational
  10. Review
  11. Article
  12. Receptor Activity-Modifying Proteins (RAMPs): New Insights and Roles.Annual review of pharmacology and toxicology · 2016
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Insights into the structure of class B GPCRs.Trends in pharmacological sciences · 2014
    Review
  20. 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

8 authors at 1 institution in 1 country.

Christy Rani R GraceThe Clayton Foundation Laboratories for Peptide Biology, The Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, CA 92037, USA.
Marilyn H Perrin
Jozsef Gulyas
Michael R Digruccio
Jeffrey P Cantle
Jean E Rivier
Wylie W Vale
Roland Riek
Salk Institute for Biological Studies · US

Funding

TARGETED DISRUPTION OF NEUROENDOCRINE GENESP01DK026741 · NIDDK · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI ZORRILLA, ERIC P, ZORRILLA, ERIC P · 1986 to 2014
$31.6M
NIDDK NIH HHS DK26741NIDDK NIH HHS P01 DK026741
6 · The paper itself

Abstract

The corticotropin releasing factor (CRF) family of ligands and their receptors coordinate endocrine, behavioral, autonomic, and metabolic responses to stress and play additional roles within the cardiovascular, gastrointestinal, and other systems. The actions of CRF and the related urocortins are mediated by activation of two receptors, CRF-R1 and CRF-R2, belonging to the B1 family of G protein-coupled receptors. The short-consensus-repeat fold (SCR) within the first extracellular domain (ECD1) of the CRF receptor(s) comprises the major ligand binding site and serves to dock a peptide ligand via its C-terminal segment, thus positioning the N-terminal segment to interact with the receptor's juxtamembrane domains to activate the receptor. Here we present the 3D NMR structure of ECD1 of CRF-R2beta in complex with astressin, a peptide antagonist. In the structure of the complex the C-terminal segment of astressin forms an amphipathic helix, whose entire hydrophobic face interacts with the short-consensus-repeat motif, covering a large intermolecular interface. In addition, the complex is characterized by intermolecular hydrogen bonds and a salt bridge. These interactions are quantitatively weighted by an analysis of the effects on the full-length receptor affinities using an Ala scan of CRF. These structural studies identify the major determinants for CRF ligand specificity and selectivity and support a two-step model for receptor activation. Furthermore, because of a proposed conservation of the fold for both the ECD1s and ligands, this structure can serve as a model for ligand recognition for the entire B1 receptor family.

Indexed as

AlanineAnimalsBinding SitesCorticotropin-Releasing HormoneLigandsModels, MolecularPeptide FragmentsPeptidesProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryReceptors, Corticotropin-Releasing HormoneSheepAlanineastressinCorticotropin-Releasing HormoneCRF receptor type 2LigandsPeptide FragmentsPeptidesReceptors, Corticotropin-Releasing Hormone

Identifiers

PMID17360332
PMCPMC1829229
OpenAlexW1979516391

What OpenQuestion holds

Textmetadata
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.