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

Aromatic anchor at an invariant hormone-receptor interface: function of insulin residue B24 with application to protein design.

The Journal of biological chemistry - 12 Dec 2014

Pandyarajan Vijay, Smith Brian J, Phillips Nelson B, Whittaker Linda, Cox Gabriella P, Wickramasinghe Nalinda, Menting John G, Wan Zhu-li, Whittaker Jonathan, Ismail-Beigi Faramarz, Lawrence Michael C, Weiss Michael A

Abstract excerpt

Crystallographic studies of insulin bound to fragments of the insulin receptor have recently defined the topography of the primary hormone-receptor interface. Here, we have investigated the role of Phe(B24), an invariant aromatic anchor at this interface and site of a human mutation causing diabetes mellitus. An extensive set of B24 substitutions has been constructed and tested for effects on receptor binding....

Read the complete abstract on PubMed

Topics

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

Share to Drug Design
Share to Hydrophobic and Hydrophilic Interactions

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

Share to Insulin

Share to Phenylalanine

Share to Protein Folding

Share to Protein Multimerization

Share to Receptor, IGF Type 1

Share to Receptor, Insulin

Source

Open in PubMed Open full text

Identifiers

PMID: 25305014
DOI: 10.1074/jbc.M114.608562
PMCID: PMC4263875

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

Aromatic anchor at an invariant hormone-receptor interface: function of insulin residue B24 with application to protein design.PMID 25305014Read ↗

Non-standard insulin design: structure-activity relationships at the periphery of the insulin receptor.Semantic proximity Read ↗

Mutations at the dimer, hexamer, and receptor-binding surfaces of insulin independently affect insulin-insulin and insulin-receptor interactions.Semantic proximity Read ↗

Human insulin analogues modified at the B26 site reveal a hormone conformation that is undetected in the receptor complex.Semantic proximity Read ↗

Paradoxical structure and function in a mutant human insulin associated with diabetes mellitus.Semantic proximity Read ↗

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

A Conserved Histidine in Insulin Is Required for the Foldability of Human ProinsulinSemantic proximity Read ↗

The structure of a mutant insulin uncouples receptor binding from protein allostery. An electrostatic block to the TR transition.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 ↗

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

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

Molecular variants and derivatives of insulin for improved glycemic control in diabetes.Semantic proximity Read ↗

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