Crystal Structure of the Extracellular Segment of Integrin αVβ3 in Complex with an Arg-Gly-Asp Ligand

By Jian-ping Xiong, T. Stehle, Rong-guang Zhang, A. Joachimiak, M. Frech, S. Goodman, M. Arnaout. Science, 2002

1,576 citations recorded by the source corpus.

Subfields: Immunology, Immunology and Allergy, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/37f2b36ef53001e05fb1de5827b23185e7461faa

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Citations in the corpus

Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling. (2002, background): “I-like domains conformation, in which the headpiece is folded over the are not analogous (Xiong et al., 2002).”
Force Measurements of the α5β1 Integrin–Fibronectin Interaction (2003, background): “Crystallographic analysis of the aVb3 integrin complexed to a cyclic RGD peptide suggests that the RGD loop in FN10 is recognized by both a5 and b1 subunits ( Xiong et al., 2002 ).”
Cilengitide: The First Anti-Angiogenic Small Molecule Drug Candidate. Design, Synthesis and Clinical Evaluation (2010, background): “In particular, integrins v 3, v 5 and 5 1 are involved in angiogenesis and metastasis of solid tumors, being excellent candidates for cancer therapy [4-7].”
Cell spreading and focal adhesion dynamics are regulated by spacing of integrin ligands. (2007, background): “These particles have a diameter of 8 nm allowing each particle to interact with only one integrin receptor (39, 40 ).”
Distribution and evolution of von Willebrand/integrin A domains: widely dispersed domains with roles in cell adhesion and elsewhere. (2002, background): “It is likely that confident conclusions regarding the presence or absence of a functional MIDAS motif will require structural analysis of the VWA domain in question in both ligand-bound and -unbound states (Xiong et al., 2002).”
Gelatinase-mediated migration and invasion of cancer cells. (2005, background): “The binding site of these ligands is either the I domain in the α subunit of integrins or a binding pocket formed by the α and β subunit together as visualized in the αVβ3 integrin structure with the RGD peptide (Xiong et al., 2002).”
Rolling Adhesion through an Extended Conformation of Integrin αLβ2 and Relation to α I and β I-like Domain Interaction (2004, methodology): “…from crystal, EM, and X-ray scattering studies on integrins that lack I domains (Adair and Yea- sion, which likely reflects a higher affinity of these antagonists for the active conformation of the 2 I-like domain.ger, 2002; Mould et al., 2003a; Takagi et al., 2002, 2003; Xiong et al., 2001, 2002).”