Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin

By L. Pellegrini, D. Burke, Frank von Delft, B. Mulloy, Tom L. Blundell. Nature, 2000

713 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/8c5aa9cd1941394b191af05aba299cc11797d7f9

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Citations in the corpus

• An Introduction to Proteoglycans and Their Localization (2012, background): “Many members of this large family bind heparan sulfate, and crystallographic studies reveal how the FGF/HS complex interacts with the FGF receptor (FGFR) kinases (Pellegrini et al. 2000; Schlessinger et al. 2000).”
• Molecular diversity of heparan sulfate. (2001, background): “In other cases, the chain may act as a template, approximating a ligand with its binding partner (13, 22, 23).”
• Structural basis for fibroblast growth factor receptor activation. (2005, background): “It was proposed that the S252W mutation results in gain-of-function by promoting a trans- to cis-isomerization of Pro253 [130] as aromatic amino acids preceding a proline have been shown to induce a high fraction of cis isomer in test peptides [136].”
• Functions of heparan sulfate proteoglycans in cell signaling during development (2004, background): “O sulfation of HS is required for FGF1-FGFR2 and FGF2FGFR1 interactions (Pellegrini et al., 2000; Schlessinger et al., 2000).”
• Demystifying Heparan Sulfate–Protein Interactions (2014, background): “The same dimerization interface observed in the FGF1 dimer has been observed in two cocrystal structures of FGF1, FGF receptor 2 (FGFR2), and dodecasaccharides derived from heparin (51, 52).”
• Endothelial PDGF-B retention is required for proper investment of pericytes in the microvessel wall. (2003, background): “Finally, HSPGs may act as coreceptors by stabilizing active ligand-receptor complexes (Pellegrini et al. 2000).”