ArticleThe Journal of cell biology2012
Crystal structure of α5β1 integrin ectodomain: atomic details of the fibronectin receptor.
Article in The Journal of cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 124 papers.
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Who cites it
124 citing papers in PubMed, 247 citations in OpenAlex.
- Shared ligand-blocking mechanism but distinct conformational modulation by α5-targeting antibodies BIIG2 and MINT1526A.Structure (London, England : 1993) · 2026Article
- Graphene Oxide-Hydroxyapatite Nanocomposite Coatings and Extracellular Matrix Protein Interactions for Enhanced Osseointegration in Dental Implants.Journal of cellular and molecular medicine · 2026Article
- Integrin α5β1 in pancreatic ductal adenocarcinoma: Tumour‒stroma crosstalk, hypoxia and therapeutic targeting.Clinical and translational medicine · 2026Review
- RPRD1A drives lenvatinib resistance in hepatocellular carcinoma via the ITGA5-FAK signaling axis.Molecular biomedicine · 2026Article
- ITGB1 Regulates Triple-Negative Breast Cancer Development by Modulating the Tumor Microenvironment.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Structural and mechanistic insights into α2β1 and α5β1 integrin targeting by bioengineered extracellular vesicles originating from lung cancer cells.Scientific reports · 2026Article
- Beyond MIDAS: AnACS omega · 2026Article
- Allosteric regulation of fibronectin binding by the anti-β1 integrin antibody TS2/16.PNAS nexus · 2026Article
- Regulation of cell dynamics by rapid integrin transport through the biosynthetic pathway.The Journal of cell biology · 2026Article
- Ruthenium Complexes in Protein Science: Heading a New Generation of Therapeutic and Analytical Tools.Angewandte Chemie (International ed. in English) · 2026Review
- SPR interaction analysis of GM3 glycan with the integrin α5β1 head domain.Glycoconjugate journal · 2026Article
- Engineered cyclic peptide targeting ITGA5 disrupts tumor-stroma interaction to overcome desmoplasia and resistance in pancreatic ductal adenocarcinoma.Acta pharmaceutica Sinica. B · 2026Article
- Novel octapeptide containing the RGD sequence as a potential anti-SARS-CoV-2 agent: design, synthesis, and theoretical studies.Amino acids · 2025Article
- Allosteric Disulfide Bridges in Integrins: The Molecular Switches of Redox Regulation of Integrin-Mediated Cell Functions.Antioxidants (Basel, Switzerland) · 2025Review
- Crossing Barriers: Advancements in Macromolecular Therapeutics for Neurodegenerative Diseases and Strategies to Overcome the Blood-Brain Barrier.ACS pharmacology & translational science · 2025Review
- De Novo Design of Integrin α5β1 Modulating Proteins to Enhance Biomaterial Properties.Advanced materials (Deerfield Beach, Fla.) · 2025Article
- Shared ligand-blocking mechanism but distinct conformational modulation by α5-targeting antibodies BIIG2 and MINT1526A.bioRxiv : the preprint server for biology · 2025Article
- Unlocking tumor barrier: annexin A2-mediated transcytosis boosts drug delivery in pancreatic and breast tumors.Nature communications · 2025Article
- Focal adhesion in the tumour metastasis: from molecular mechanisms to therapeutic targets.Biomarker research · 2025Review
- Luminescent sensing of conformational integrin activation in living cells.Cell reports · 2025Article
64 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Integrin α5β1 is a major cellular receptor for the extracellular matrix protein fibronectin and plays a fundamental role during mammalian development. A crystal structure of the α5β1 integrin headpiece fragment bound by an allosteric inhibitory antibody was determined at a 2.9-Å resolution both in the absence and presence of a ligand peptide containing the Arg-Gly-Asp (RGD) sequence. The antibody-bound β1 chain accommodated the RGD ligand with very limited structural changes, which may represent the initial step of cell adhesion mediated by nonactivated integrins. Furthermore, a molecular dynamics simulation pointed to an important role for Ca(2+) in the conformational coupling between the ligand-binding site and the rest of the molecule. The RGD-binding pocket is situated at the center of a trenchlike exposed surface on the top face of α5β1 devoid of glycosylation sites. The structure also enabled the precise prediction of the acceptor residue for the auxiliary synergy site of fibronectin on the α5 subunit, which was experimentally confirmed by mutagenesis and kinetic binding assays.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.