Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Mapping spatial approximations between the amino terminus of secretin and each of the extracellular loops of its receptor using cysteine trapping.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology - 1 Dec 2012

Dong Maoqing, Xu Xiequn, Ball Alicja M, Makhoul Joshua A, Lam Polo C-H, Pinon Delia I, Orry Andrew, Sexton Patrick M, Abagyan Ruben, Miller Laurence J

Abstract excerpt

While it is evident that the carboxyl-terminal region of natural peptide ligands bind to the amino-terminal domain of class B GPCRs, how their biologically critical amino-terminal regions dock to the receptor is unclear. We utilize cysteine trapping to systematically explore spatial approximations among residues in the first five positions of secretin and in every position within the receptor extracellular loops...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Binding, Competitive
Share to Cricetulus

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Disulfides

Share to Phenylalanine

Share to Proline

Share to Protein Interaction Mapping

Share to Receptors, G-Protein-Coupled

Share to Tryptophan

Source

Open in PubMed Open full text

Identifiers

PMID: 22964305
DOI: 10.1096/fj.12-212399
PMCID: PMC3509059

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mapping spatial approximations between the amino terminus of secretin and each of the extracellular loops of its receptor using cysteine trapping.PMID 22964305Read ↗

Paired cysteine mutagenesis to establish the pattern of disulfide bonds in the functional intact secretin receptor.Semantic proximity Read ↗

Spatial approximation between two residues in the mid-region of secretin and the amino terminus of its receptor. Incorporation of seven sets of such constraints into a three-dimensional model of the agonist-bound secretin receptor.Semantic proximity Read ↗

Impact of secretin receptor homo-dimerization on natural ligand binding.Semantic proximity Read ↗

Molecular approximation between residue 10 of secretin and its receptor demonstrated by photoaffinity labeling.Semantic proximity Read ↗

Dynamics of the Second Extracellular Loop Control Transducer Coupling of Peptide-Activated GPCRs.Semantic proximity Read ↗

Insights into the structure and molecular basis of ligand docking to the G protein-coupled secretin receptor using charge-modified amino-terminal agonist probes.Semantic proximity Read ↗

Functional segregation of the highly conserved basic motifs within the third endoloop of the human secretin receptor.Semantic proximity Read ↗

Understanding the molecular functions of the second extracellular loop (ECL2) of the calcitonin gene-related peptide (CGRP) receptor using a comprehensive mutagenesis approach.Semantic proximity Read ↗

Differential determinants for coupling of distinct G proteins with the class B secretin receptor.Semantic proximity Read ↗

EGF‐like and Other Disulfide‐rich Microdomains as Therapeutic ScaffoldsSemantic proximity Read ↗

The unique extracellular disulfide loop of the glycine receptor is a principal ligand binding element.Semantic proximity Read ↗

Disulfide bonds determine growth hormone receptor folding, dimerisation and ligand binding.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.