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

Delineating a Ca2+ binding pocket within the venus flytrap module of the human calcium-sensing receptor.

The Journal of biological chemistry - 11 Nov 2005

Silve Caroline, Petrel Christophe, Leroy Christine, Bruel Henri, Mallet Eric, Rognan Didier, Ruat Martial

Abstract excerpt

The Ca(2+)-sensing receptor (CaSR) belongs to the class III G-protein-coupled receptors (GPCRs), which include receptors for pheromones, amino acids, sweeteners, and the neurotransmitters glutamate and gamma-aminobutyric acid (GABA). These receptors are characterized by a long extracellular amino-terminal domain called a Venus flytrap module (VFTM) containing the ligand binding pocket. To elucidate the molecular...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Binding Sites

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

Share to Calcium

Share to Pedigree

Share to Phylogeny

Share to Receptors, AMPA

Share to Receptors, Calcium-Sensing

Source

Identifiers

PMID: 16147994
DOI: 10.1074/jbc.M506263200

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

Delineating a Ca2+ binding pocket within the venus flytrap module of the human calcium-sensing receptor.PMID 16147994Read ↗

Naturally occurring mutations of the extracellular Ca2+-sensing receptor: implications for its structure and function.Semantic proximity Read ↗

Identification of 70 calcium-sensing receptor mutations in hyper- and hypo-calcaemic patients: evidence for clustering of extracellular domain mutations at calcium-binding sites.Semantic proximity Read ↗

Recent advances in calcium-sensing receptor structures and signaling pathways.Semantic proximity Read ↗

Evolutionary history of calcium-sensing receptors unveils hyper/hypocalcemia-causing mutations.Semantic proximity Read ↗

Evolutionary History of Calcium-Sensing Receptors Unveils Hyper/Hypocalcemia-Causing MutationsSemantic proximity Read ↗

Structural basis for regulation of human calcium-sensing receptor by magnesium ions and an unexpected tryptophan derivative co-agonist.Semantic proximity Read ↗

Identification of the modulatory Ca2+-binding sites of acid-sensing ion channel 1a.Semantic proximity Read ↗

Structure and function of the human calcium-sensing receptor: insights from natural and engineered mutations and allosteric modulators.Semantic proximity Read ↗

Determination of the melanocortin-4 receptor structure identifies Ca2+ as a cofactor for ligand binding.Semantic proximity Read ↗

A double mutation in the extracellular Ca2+-sensing receptor's venus flytrap domain that selectively disables L-amino acid sensing.Semantic proximity Read ↗

Molecular and clinical insights from studies of calcium-sensing receptor mutationsSemantic proximity Read ↗

Ancestral reconstruction of the ligand-binding pocket of Family C G protein-coupled receptors.Semantic proximity Read ↗

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