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

Decoding the cryptic active conformation of a protein by synthetic photoscanning: insulin inserts a detachable arm between receptor domains.

The Journal of biological chemistry - 22 May 2009

Xu Bin, Huang Kun, Chu Ying-Chi, Hu Shi-Quan, Nakagawa Satoe, Wang Shuhua, Wang Run-Ying, Whittaker Jonathan, Katsoyannis Panayotis G, Weiss Michael A

Abstract excerpt

Proteins evolve in a fitness landscape encompassing a complex network of biological constraints. Because of the interrelation of folding, function, and regulation, the ground-state structure of a protein may be inactive. A model is provided by insulin, a vertebrate hormone central to the control of metabolism. Whereas native assembly mediates storage within pancreatic beta-cells, the active conformation of...

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Regulation
Share to Chymotrypsin

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cross-Linking Reagents

Share to Insulin

Share to Peptide Mapping

Share to Receptor, Insulin

Share to Sus scrofa

Source

Open in PubMed Open full text

Identifiers

PMID: 19321435
DOI: 10.1074/jbc.M900087200
PMCID: PMC2682907

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Decoding the cryptic active conformation of a protein by synthetic photoscanning: insulin inserts a detachable arm between receptor domains.PMID 19321435Read ↗

Diabetes-associated mutations in insulin identify invariant receptor contacts.Semantic proximity Read ↗

α-Helical element at the hormone-binding surface of the insulin receptor functions as a signaling element to activate its tyrosine kinase.Semantic proximity Read ↗

The A-chain of insulin contacts the insert domain of the insulin receptor. Photo-cross-linking and mutagenesis of a diabetes-related crevice.Semantic proximity Read ↗

Diabetes-associated mutations in human insulin: crystal structure and photo-cross-linking studies of a-chain variant insulin Wakayama.Semantic proximity Read ↗

Diabetes-associated mutations in insulin: consecutive residues in the B chain contact distinct domains of the insulin receptor.Semantic proximity Read ↗

Genetically encoded photocross-linkers determine the biological binding site of exendin-4 peptide in the N-terminal domain of the intact human glucagon-like peptide-1 receptor (GLP-1R).Semantic proximity Read ↗

Structural Lessons From the Mutant Proinsulin Syndrome.Semantic proximity Read ↗

A Single-Chain Photoswitchable CRISPR-Cas9 Architecture for Light-Inducible Gene Editing and Transcription.Semantic proximity Read ↗

Structural analysis of proinsulin hexamer assembly by hydroxyl radical footprinting and computational modeling.Semantic proximity Read ↗

The road to the first, fully active and more stable human insulin variant with an additional disulfide bond.Semantic proximity Read ↗

A Model for the Molecular Mechanism of an Engineered Light-Driven Protein Machine.Semantic proximity Read ↗

Design of an insulin analog with enhanced receptor binding selectivity: rationale, structure, and therapeutic implications.Semantic proximity Read ↗

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