Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity

Article Abstract:

Crystal structures of two fibroblast growth factor (FGF)-FGFR complexes are discussed. They have been found to show the determinants of ligand-receptor specificity. Crystal structures of FGF1 and FGF2 complexed with the ligand-binding domains (immunoglobulin-like domains 2(D2) and 3 (D3)) of FGF receptor 1 and and FGFR2, respectively, have been determined. Valuable insights into molecular mechanisms that manage FGF-FGFR binding specificity have been found.

Genetic aspects, Cytochemistry, Ligands (Biochemistry), Immunocytochemistry, Mammals, Molecular genetics

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Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism

Article Abstract:

The fibroblast growth factor receptor 1's (FGFR1K) crystal structure shows a a second three-dimensional structure of a receptor protein tyrosine kinase (PTK) domain. In FGFR1K, the activation loop is disposed such that the binding site for substrate peptides is blocked by Arg-661 and PTK-invariant Pro-663 while the ATP binding site is accessible. The autoinhibition seen in FGFR1K will seem to be weaker than in the insulin receptor tyrosine kinase (IRK) because the residues in the FGFR1K activation loop are engaged in a lesser number of specific interactions. Another reason is the ATP site's accessibility.

Protein kinases, Tyrosine

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Structural basis for FGF receptor dimerization and activation

Article Abstract:

Structural basis for fibroblast growth factor (FGF) receptor activation and dimerization is discussed. Crystal structure of FGF2 bound to a naturally occurring variant of FGF receptor 1 (FGFR1) made up of immunoglobulin-like domains 2 and 3 has been determined at 2.8-angstrom resolution. A generalized model for FGF- and heparin-induced FGFR dimerization has been developed based on the crystal structure and on much biochemical data.

Analysis, Proteins, Protein binding, Cell receptors, Crystals, Crystal structure, Heparin, Proteoglycans

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