ArticleThe Journal of biological chemistry2016
β-Subunit Binding Is Sufficient for Ligands to Open the Integrin αIIbβ3 Headpiece.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 35 citations in OpenAlex.
- EMoMiS: A pipeline for epitope-based molecular mimicry search in protein structures with potential applications to SARS-CoV-2.Computational and structural biotechnology journal · 2026Article
- MnBiophysical journal · 2025Article
- Application of Funnel Metadynamics to the Platelet Integrin αIIbβ3 in Complex with an RGD Peptide.International journal of molecular sciences · 2024Article
- Conjecturing about Small-Molecule Agonists and Antagonists of α4β1 Integrin: From Mechanistic Insight to Potential Therapeutic Applications.Biomedicines · 2024Review
- Article
- Design and Pharmacological Characterization of αJournal of medicinal chemistry · 2023Article
- Structure-Based Discovery of a Novel Class of Small-Molecule Pure Antagonists of Integrin αVβ3.Journal of chemical information and modeling · 2022Article
- Physical, Mechanical, and Biological Properties of Fibrin Scaffolds for Cartilage Repair.International journal of molecular sciences · 2022Review
- Regulation of integrin α5β1 conformational states and intrinsic affinities by metal ions and the ADMIDAS.Molecular biology of the cell · 2022Article
- Humanized β2 Integrin-Expressing Hoxb8 Cells Serve as Model to Study Integrin Activation.Cells · 2022Article
- Reconstitution of Functional Integrin αIIbβ3 and Its Activation in Plasma Membrane-Mimetic Lipid Environments.Membranes · 2021Article
- Structural mechanism of laminin recognition by integrin.Nature communications · 2021Article
- Dominant role of αIIbβ3 in platelet interactions with cross-linked fibrin fragment D-dimer.Blood advances · 2020Article
- Novel Pure αVβ3 Integrin Antagonists That Do Not Induce Receptor Extension, Prime the Receptor, or Enhance Angiogenesis at Low Concentrations.ACS pharmacology & translational science · 2019Article
- Autonomous conformational regulation of βProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Low-affinity binding inMolecular biology of the cell · 2017Article
- Article
- Relating conformation to function in integrin α5β1.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The platelet integrin αIIbβ3 binds to a KQAGDV motif at the fibrinogen γ-chain C terminus and to RGD motifs present in loops in many extracellular matrix proteins. These ligands bind in a groove between the integrin α and β-subunits; the basic Lys or Arg side chain hydrogen bonds to the αIIb-subunit, and the acidic Asp side chain coordinates to a metal ion held by the β3-subunit. Ligand binding induces headpiece opening, with conformational change in the β-subunit. During this opening, RGD slides in the ligand-binding pocket toward αIIb, with movement of the βI-domain β1-α1 loop toward αIIb, enabling formation of direct, charged hydrogen bonds between the Arg side chain and αIIb. Here we test whether ligand interactions with β3 suffice for stable ligand binding and headpiece opening. We find that the AGDV tetrapeptide from KQAGDV binds to the αIIbβ3 headpiece with affinity comparable with the RGDSP peptide from fibronectin. AGDV induced complete headpiece opening in solution as shown by increase in hydrodynamic radius. Soaking of AGDV into closed αIIbβ3 headpiece crystals induced intermediate states similarly to RGDSP. AGDV has very little contact with the α-subunit. Furthermore, as measured by epitope exposure, AGDV, like the fibrinogen γ C-terminal peptide and RGD, caused integrin extension on the cell surface. Thus, pushing by the β3-subunit on Asp is sufficient for headpiece opening and ligand sliding, and no pulling by the αIIb subunit on Arg is required.
Indexed as
Identifiers
What OpenQuestion holds
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.