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

Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity.

Journal of molecular biology - 17 Apr 1998

Clackson T, Ultsch M H, Wells J A, de Vos A M

Abstract excerpt

The designed G120R mutant of human growth hormone (hGH) is an antagonist and can bind only one molecule of the growth hormone receptor. We have determined the crystal structure of the 1:1 complex between this mutant and the receptor extracellular domain (hGHbp) at 2.6 A resolution, and used it to guide a detailed survey of the structural and functional basis for hormone-receptor recognition. The overall structure...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Crystallography, X-Ray

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

Share to Epitopes

Share to Kinetics

Share to Models, Molecular

Share to Mutation

Share to Protein Binding

Share to Protein Conformation

Source

Identifiers

PMID: 9571026
DOI: 10.1006/jmbi.1998.1669

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

Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity.PMID 9571026Read ↗

Binding in the growth hormone receptor complex.Semantic proximity Read ↗

Crystals of human growth hormone-receptor complexes. Extracellular domains of the growth hormone and prolactin receptors and a hormone mutant designed to prevent receptor dimerization.Semantic proximity Read ↗

Structure of a phage display-derived variant of human growth hormone complexed to two copies of the extracellular domain of its receptor: evidence for strong structural coupling between receptor binding sites.Semantic proximity Read ↗

Human growth hormone and extracellular domain of its receptor: crystal structure of the complex.Semantic proximity Read ↗

The functional binding epitope of a high affinity variant of human growth hormone mapped by shotgun alanine-scanning mutagenesis: insights into the mechanisms responsible for improved affinity.Semantic proximity Read ↗

Site2 binding energetics of the regulatory step of growth hormone-induced receptor homodimerization.Semantic proximity Read ↗

Increased site 1 affinity improves biopotency of porcine growth hormone. Evidence against diffusion dependent receptor dimerization.Semantic proximity Read ↗

The crystal structure of affinity-matured human growth hormone at 2 A resolution.Semantic proximity Read ↗

A systematic mutational analysis of hormone-binding determinants in the human growth hormone receptor.Semantic proximity Read ↗

Determination of the energetics governing the regulatory step in growth hormone-induced receptor homodimerization.Semantic proximity Read ↗

Mapping the Functional Epitopes of Human Growth Hormone: Integrating Structural and Evolutionary Data with Clinical VariantsSemantic proximity Read ↗

Structural and Evolutionary Analysis of Human Growth Hormone VariantsSemantic proximity Read ↗

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