ArticleThe Biochemical journal2004
Novel activating and inactivating mutations in the integrin beta1 subunit A domain.
Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
17 citing papers in PubMed, 27 citations in OpenAlex.
- DynMoCo: A novel AI framework to reveal modular substructures of protein from molecular dynamics.Biophysical journal · 2026Article
- DynMoCo: a Novel AI Framework to Reveal Modular Substructures of Protein From Molecular Dynamics.bioRxiv : the preprint server for biology · 2026Article
- Contributions of the individual domains of αCytoskeleton (Hoboken, N.J.) · 2024Article
- A pivotal role for a conserved bulky residue at the α1-helix of the αI integrin domain in ligand binding.The Journal of biological chemistry · 2017Article
- Ligand-induced Epitope Masking: DISSOCIATION OF INTEGRIN α5β1-FIBRONECTIN COMPLEXES ONLY BY MONOCLONAL ANTIBODIES WITH AN ALLOSTERIC MODE OF ACTION.The Journal of biological chemistry · 2016Article
- Complete integrin headpiece opening in eight steps.The Journal of cell biology · 2013Article
- The unique disulfide bond-stabilized W1 β4-β1 loop in the α4 β-propeller domain regulates integrin α4β7 affinity and signaling.The Journal of biological chemistry · 2013Article
- Role of altered sialylation of the I-like domain of beta1 integrin in the binding of fibronectin to beta1 integrin: thermodynamics and conformational analyses.Biophysical journal · 2010Article
- Integrin activation dynamics between the RGD-binding site and the headpiece hinge.The Journal of biological chemistry · 2009Article
- Targeted molecular dynamics reveals overall common conformational changes upon hybrid domain swing-out in beta3 integrins.Proteins · 2009Article
- Distinct roles of beta1 metal ion-dependent adhesion site (MIDAS), adjacent to MIDAS (ADMIDAS), and ligand-associated metal-binding site (LIMBS) cation-binding sites in ligand recognition by integrin alpha2beta1.The Journal of biological chemistry · 2008Article
- Ubiquitin lysine 63 chain forming ligases regulate apical dominance in Arabidopsis.The Plant cell · 2007Article
- Tests of the extension and deadbolt models of integrin activation.The Journal of biological chemistry · 2007Article
- Integrin structures and conformational signaling.Current opinion in cell biology · 2006Review
- Dual functionality of the anti-beta1 integrin antibody, 12G10, exemplifies agonistic signalling from the ligand binding pocket of integrin adhesion receptors.The Journal of biological chemistry · 2005Article
- Evidence that monoclonal antibodies directed against the integrin beta subunit plexin/semaphorin/integrin domain stimulate function by inducing receptor extension.The Journal of biological chemistry · 2005Article
- Identification of integrin beta subunit mutations that alter heterodimer function in situ.Molecular biology of the cell · 2004Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ligand-binding activity of integrins is regulated by shape changes that convert these receptors from a resting (or inactive) state to an active state. However, the precise conformational changes that take place in head region of integrins (the site of ligand binding) during activation are not well understood. The portion of the integrin beta subunit involved in ligand recognition contains a von Willebrand factor type A domain, which comprises a central beta-sheet surrounded by seven alpha helices (alpha1-alpha7). Using site-directed mutagenesis, we show here that point mutation of hydrophobic residues in the alpha1 and alpha7 helices (which would be predicted to increase the mobility of these helices) markedly increases the ligand-binding activity of both integrins alpha5beta1 and alpha4beta1. In contrast, mutation of a hydrophilic residue near the base of the alpha1 helix decreases activity and also suppresses exposure of activation epitopes on the underlying hybrid domain. Our results provide new evidence that shifts of the alpha1 and alpha7 helices are involved in activation of the A domain. Although these changes are grossly similar to those defined in the A domains found in some integrin alpha subunits, movement of the alpha1 helix appears to play a more prominent role in betaA domain activation.
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Registered trials
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.