ArticleBiophysical journal2008
Key interactions in integrin ectodomain responsible for global conformational change detected by elastic network normal-mode analysis.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- The Integrin Receptors: From Discovery to Structure to Medicines.Immunological reviews · 2025Review
- Cryo-EM structures of full-length integrin αIIbβ3 in native lipids.Nature communications · 2023Article
- Multiscale models of integrins and cellular adhesions.Current opinion in structural biology · 2023Review
- Conformational dynamics of a multidomain protein by neutron scattering and computational analysis.Biophysical journal · 2021Article
- When Stiffness Matters: Mechanosensing in Heart Development and Disease.Frontiers in cell and developmental biology · 2020Review
- 2D hybrid analysis: Approach for building three-dimensional atomic model by electron microscopy image matching.Scientific reports · 2017Article
- Conformational shift in the closed state of GroEL induced by ATP-binding triggers a transition to the open state.Biophysics and physicobiology · 2016Article
- Giant cadherins Fat and Dachsous self-bend to organize properly spaced intercellular junctions.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- α(V)β(3) integrin crystal structures and their functional implications.Biochemistry · 2012Article
- Identification of integrin beta subunit mutations that alter affinity for extracellular matrix ligand.The Journal of biological chemistry · 2011Article
- Molecular insight into human platelet antigens: structural and evolutionary conservation analyses offer new perspective to immunogenic disorders.Transfusion · 2011Article
- Molecular dynamics simulations of forced unbending of integrin α(v)β₃.PLoS computational biology · 2011Article
- Structural requirements for activation in alphaIIb beta3 integrin.The Journal of biological chemistry · 2010Article
- Targeted molecular dynamics reveals overall common conformational changes upon hybrid domain swing-out in beta3 integrins.Proteins · 2009Article
- Crystal structure of the complete integrin alphaVbeta3 ectodomain plus an alpha/beta transmembrane fragment.The Journal of cell biology · 2009Article
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Authors and funding
5 authors.
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Abstract
Integrin, a membrane protein with a huge extracellular domain, participates in cell-cell and cell-extracellular-matrix interactions for metazoan. A group of integrins is known to perform a large-scale structural change when the protein is activated, but the activation mechanism and generality of the conformational change remain to be elucidated. We performed normal-mode analysis of the elastic network model on integrin alpha(V)beta(3) ectodomain in the bent form and identified key residues that influenced molecular motions. Iterative normal-mode calculations demonstrated that the specific nonbonded interactions involving the key residues work as a snap to keep integrin in the bent form. The importance of the key residues for the conformational change was further verified by mutation experiments, in which integrin alpha(IIb)beta(3) was used. The conservation pattern of amino acid residues among the integrin family showed that the characteristic pattern of residues seen around these key residues is found in the limited groups of integrin beta-chains. This conservation pattern suggests that the molecular mechanism of the conformational change relying on the interactions found in integrin alpha(V)beta(3) is unique to the limited types of integrins.
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