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

Eleven amino acids (Lys-201 to Lys-211) and 9 amino acids (Gly-222 to Leu-230) in the human thyrotropin receptor are involved in ligand binding.

The Journal of biological chemistry - 15 Aug 1991

Nagayama Y, Russo D, Wadsworth H L, Chazenbalk G D, Rapoport B

Abstract excerpt

Our previous studies involving chimeric thyrotropin-lutropin/choriogonadotropin (TSH-LH/CG) receptors suggest that multiple segments spanning the entire extracellular domain of the human TSH receptor contribute to the TSH binding site. Nevertheless, the mid-region (segment C, amino acid residues 171-260) of the receptor extracellular domain is particularly important in TSH binding. In the present studies, we...

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 Cricetinae

Share to Molecular Sequence Data

Share to Mutation

Share to Plasmids

Share to Transfection

Source

Identifiers

PMID: 1651314

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

Eleven amino acids (Lys-201 to Lys-211) and 9 amino acids (Gly-222 to Leu-230) in the human thyrotropin receptor are involved in ligand binding.PMID 1651314Read ↗

An insertion in the human thyrotropin receptor critical for high affinity hormone binding.Semantic proximity Read ↗

Thyrotropin and Homologous Glycoprotein Hormone Receptors: Structural and Functional Aspects of Extracellular Signaling MechanismsSemantic proximity Read ↗

Extended and Structurally Supported Insights into Extracellular Hormone Binding, Signal Transduction and Organization of the Thyrotropin ReceptorSemantic proximity Read ↗

The functional significance of the second extracellular loop of thyrotropin receptor in thyrotropin- and thyroid stimulating antibody-dependent signal transduction.Semantic proximity Read ↗

Asp330 and Tyr331 in the C-terminal cysteine-rich region of the luteinizing hormone receptor are key residues in hormone-induced receptor activation.Semantic proximity Read ↗

A hydrophobic cluster in the center of the third extracellular loop is important for thyrotropin receptor signaling.Semantic proximity Read ↗

Determination of residues important in hormone binding to the extracellular domain of the luteinizing hormone/chorionic gonadotropin receptor by site-directed mutagenesis and modeling.Semantic proximity Read ↗

Point mutations of the thyrotropin receptor determining structural requirements for its ability to bind thyrotropin and to stimulate adenylate cyclase activity.Semantic proximity Read ↗

Defining structural and functional dimensions of the extracellular thyrotropin receptor region.Semantic proximity Read ↗

Structural differences in the hinge region of the glycoprotein hormone receptors: evidence from the sulfated tyrosine residues.Semantic proximity Read ↗

Structural determinants for g protein activation and selectivity in the second intracellular loop of the thyrotropin receptor.Semantic proximity Read ↗

Influence of the hinge region and its adjacent domains on binding and signaling patterns of the thyrotropin and follitropin receptor.Semantic proximity Read ↗

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