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

Identification of amino acid residues that form part of the ligand-binding pocket of integrin alpha5 beta1.

The Journal of biological chemistry - 2 Oct 1998

Mould A P, Burrows L, Humphries M J

Abstract excerpt

Arg-Arg-Glu-Thr-Ala-Trp-Ala (RRETAWA) is a novel ligand peptide for integrin alpha5 beta1, which blocks alpha5 beta1-mediated cell adhesion to fibronectin (Koivunen, E., Wang, B., and Ruoslahti, E. (1994) J. Cell Biol. 124, 373-380). Here we have localized the binding site for RRETAWA on alpha5 beta1 using inhibitory monoclonal antibodies (mAbs) and site-directed mutagenesis. A cyclic peptide containing this...

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 Antibodies, Monoclonal
Share to Binding Sites

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

Share to Molecular Sequence Data

Share to Mutagenesis, Site-Directed

Share to Mutation

Share to Protein Binding

Source

Identifiers

PMID: 9748233
DOI: 10.1074/jbc.273.40.25664

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

Identification of amino acid residues that form part of the ligand-binding pocket of integrin alpha5 beta1.PMID 9748233Read ↗

Molecular basis of ligand recognition by integrin alpha5beta 1. II. Specificity of arg-gly-Asp binding is determined by Trp157 OF THE alpha subunit.Semantic proximity Read ↗

Fine mapping of inhibitory anti-alpha5 monoclonal antibody epitopes that differentially affect integrin-ligand binding.Semantic proximity Read ↗

Mapping the ligand-binding pocket of integrin alpha5beta1 using a gain-of-function approach.Semantic proximity Read ↗

Amino acid mutagenesis within ligand-binding loops in alpha v confers loss-of-function or gain-of-function phenotype on integrin alpha v beta 3.Semantic proximity Read ↗

Molecular Basis of the Ligand Binding Specificity of αvβ8 Integrin.Semantic proximity Read ↗

Epitopes in α8β1 and other RGD-binding integrins delineate classes of integrin-blocking antibodies and major binding loops in α subunits.Semantic proximity Read ↗

Distinct structural requirements for binding of the integrins alphavbeta6, alphavbeta3, alphavbeta5, alpha5beta1 and alpha9beta1 to osteopontin.Semantic proximity Read ↗

Multiple loop structures critical for ligand binding of the integrin alpha4 subunit in the upper face of the beta-propeller mode 1.Semantic proximity Read ↗

Structural analysis of peptide binding to integrins for cancer detection and treatmentSemantic proximity Read ↗

A novel region of the alpha4 integrin subunit with a modulatory role in VLA-4-mediated cell adhesion to fibronectin.Semantic proximity Read ↗

Integrin activation involves a conformational change in the alpha 1 helix of the beta subunit A-domain.Semantic proximity Read ↗

Fibrinogen binds to integrin alpha(5)beta(1) via the carboxyl-terminal RGD site of the Aalpha-chain.Semantic proximity Read ↗

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