ArticleThe Journal of biological chemistry2010
Effects of limiting extension at the alphaIIb genu on ligand binding to integrin alphaIIbbeta3.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 20 citations in OpenAlex.
- Structural basis for the differential recognition of integrin αvβ3 by rhodostomin and trimucrin.Communications biology · 2026Article
- Electron microscopy shows that binding of monoclonal antibody PT25-2 primes integrin αIIbβ3 for ligand binding.Blood advances · 2021Article
- In silico analysis of structural modifications in and around the integrin αIIb genu caused by ITGA2B variants in human platelets with emphasis on Glanzmann thrombasthenia.Molecular genetics & genomic medicine · 2018Article
- αIIbβ3 variants defined by next-generation sequencing: predicting variants likely to cause Glanzmann thrombasthenia.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Integrin αII b tail distal of GFFKR participates in inside-out αII b β3 activation.Journal of thrombosis and haemostasis : JTH · 2014Article
- Redox-relevant aspects of the extracellular matrix and its cellular contacts via integrins.Antioxidants & redox signaling · 2014Review
- The mechanism of kindlin-mediated activation of integrin αIIbβ3.Current biology : CB · 2013Article
- Epitope mapping for monoclonal antibody reveals the activation mechanism for αVβ3 integrin.PloS one · 2013Article
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- Heparin modulates the conformation and signaling of platelet integrin αIIbβ3.Thrombosis research · 2012Article
- Reconstruction of integrin activation.Blood · 2012Review
- Structural requirements for activation in alphaIIb beta3 integrin.The Journal of biological chemistry · 2010Article
- Forcing switch from short- to intermediate- and long-lived states of the alphaA domain generates LFA-1/ICAM-1 catch bonds.The Journal of biological chemistry · 2010Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Structural data of integrin alphaIIbbeta3 have been interpreted as supporting a model in which: 1) the receptor exists primarily in a "bent," low affinity conformation on unactivated platelets and 2) activation induces an extended, high affinity conformation prior to, or following, ligand binding. Previous studies found that "clasping" the alphaIIb head domain to the beta3 tail decreased fibrinogen binding. To study the role of alphaIIb extension about the genu, we introduced a disulfide "clamp" between the alphaIIb thigh and calf-1 domains. Clamped alphaIIbbeta3 had markedly reduced ability to bind the large soluble ligands fibrinogen and PAC-1 when activated with monoclonal antibody (mAb) PT25-2 but not when activated by Mn(2+) or by coexpressing the clamped alphaIIb with a beta3 subunit containing the activating mutation N339S. The clamp had little effect on the binding of the snake venom kistrin (M(r) 7,500) or alphaIIbbeta3-mediated adhesion to immobilized fibrinogen, but it did diminish the enhanced binding of mAb AP5 in the presence of kistrin. Collectively, our studies support a role for alphaIIb extension about the genu in the binding of ligands of 340,000 and 900,000 M(r) with mAb-induced activation but indicate that it is not an absolute requirement. Our data are consistent with alphaIIb extension resulting in increased access to the ligand-binding site and/or facilitating the conformational change(s) in beta3 that affect the intrinsic affinity of the binding pocket for ligand.
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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.