Journal ArticleDOI
Crystal Structure of the Extracellular Segment of Integrin αVβ3 in Complex with an Arg-Gly-Asp Ligand
Jian-Ping Xiong,Thilo Stehle,Rongguang Zhang,Andrzej Joachimiak,Matthias Frech,Simon L. Goodman,M. Amin Arnaout +6 more
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TLDR
The crystal structure of the extracellular segment of integrin αVβ3 in complex with a cyclic peptide presenting the Arg-Gly-Asp sequence is reported and ligand binding induces small changes in the orientation of αV relative to β3.Abstract:
The structural basis for the divalent cation-dependent binding of heterodimeric alphabeta integrins to their ligands, which contain the prototypical Arg-Gly-Asp sequence, is unknown. Interaction with ligands triggers tertiary and quaternary structural rearrangements in integrins that are needed for cell signaling. Here we report the crystal structure of the extracellular segment of integrin alphaVbeta3 in complex with a cyclic peptide presenting the Arg-Gly-Asp sequence. The ligand binds at the major interface between the alphaV and beta3 subunits and makes extensive contacts with both. Both tertiary and quaternary changes are observed in the presence of ligand. The tertiary rearrangements take place in betaA, the ligand-binding domain of beta3; in the complex, betaA acquires two cations, one of which contacts the ligand Asp directly and the other stabilizes the ligand-binding surface. Ligand binding induces small changes in the orientation of alphaV relative to beta3.read more
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Integrins: Bidirectional, Allosteric Signaling Machines
TL;DR: Current structural and cell biological data suggest models for how integrins transmit signals between their extracellular ligand binding adhesion sites and their cytoplasmic domains, which link to the cytoskeleton and to signal transduction pathways.
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Self-assembled monolayers of thiolates on metals as a form of nanotechnology.
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RGD modified polymers: biomaterials for stimulated cell adhesion and beyond
TL;DR: The impacts of RGD peptide surface density, spatial arrangement as well as integrin affinity and selectivity on cell responses like adhesion and migration are discussed.
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Structural Basis of Integrin Regulation and Signaling
TL;DR: This review focuses on integrin structure as it relates to affinity modulation, ligand binding, outside-in signaling, and cell surface distribution dynamics.
References
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Journal ArticleDOI
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Axel T. Brunger,Axel T. Brunger,Paul D. Adams,G M Clore,W. L. DeLano,Piet Gros,R.W. Grosse-Kunstleve,R.W. Grosse-Kunstleve,Jiansheng Jiang,J. Kuszewski,Michael Nilges,Navraj S. Pannu,Randy J. Read,Luke M. Rice,Thomas Simonson,Gregory L. Warren +15 more
TL;DR: The Crystallography & NMR System (CNS) as mentioned in this paper is a software suite for macromolecular structure determination by X-ray crystallography or solution nuclear magnetic resonance (NMR) spectroscopy.
Journal ArticleDOI
Ligand binding to integrins.
TL;DR: The number of integrins and the remarkable breadth of their cellular distribution support the statement that the phenotype of virtually every cell is uniquely influenced by its display ofintegrins.
Journal ArticleDOI
Crystal Structure of the Extracellular Segment of Integrin αVβ3
Jian-Ping Xiong,Thilo Stehle,Beate Diefenbach,Rongguang Zhang,Reinhardt Dunker,David L. Scott,Andrzej Joachimiak,Simon L. Goodman,M. Amin Arnaout +8 more
TL;DR: In this paper, the authors solved the crystal structure of the extracellular portion of integrin αVβ3 at 3.1 A resolution, showing that the αβ heterodimeric receptors mediate divalent cation-dependent cell-cell and cell-matrix adhesion through tightly regulated interactions with ligands.
Journal ArticleDOI
Structural Basis of Collagen Recognition by Integrin α2β1
Jonas Emsley,C. Graham Knight,Richard W. Farndale,Michael J. Barnes,Robert C. Liddington,Robert C. Liddington +5 more
TL;DR: The crystal structure of a complex between the I domain of integrin alpha2beta1 and a triple helical collagen peptide containing a critical GFOGER motif is determined, suggesting both a basis for affinity regulation and a pathway for signal transduction.
Journal ArticleDOI
Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18).
TL;DR: The high resolution crystal structure of the A domain from the alpha chain of integrin CR3 is determined and it is suggested that the beta subunits of integrins contain a MIDAS motif within a modified A domain.