1FGK

CRYSTAL STRUCTURE OF THE TYROSINE KINASE DOMAIN OF FIBROBLAST GROWTH FACTOR RECEPTOR 1

Summary for 1FGK

• Entry DOI: 10.2210/pdb1fgk/pdb
• Descriptor: FGF RECEPTOR 1 (2 entities in total)
• Functional Keywords: transferase, tyrosine-protein kinase, atp-binding, phosphorylation, receptor, phosphotransferase
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Single-pass type I membrane protein: P11362
• Total number of polymer chains: 2
• Total formula weight: 70617.23

Authors

Mohammadi, M.,Schlessinger, J.,Hubbard, S.R. (deposition date: 1997-02-08, release date: 1997-07-23, Last modification date: 2024-02-07)

Primary citation

Mohammadi, M.,Schlessinger, J.,Hubbard, S.R.
Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism.
Cell(Cambridge,Mass.), 86:577-587, 1996

PubMed Abstract: The crystal structure of the tyrosine kinase domain of fibroblast growth factor receptor 1 (FGFR1K) has been determined in its unliganded form to 2.0 angstroms resolution and in complex with with an ATP analog to 2.3 angstrosms A resolution. Several features distinguish the structure of FGFR1K from that of the tyrosine kinase domain of the insulin receptor. Residues in the activation loop of FGFR1K appear to interfere with substrate peptide binding but not with ATP binding, revealing a second and perhaps more general autoinhibitory mechanism for receptor tyrosine kinases. In addition, a dimeric form of FGFR1K observed in the crystal structure may provide insights into the molecular mechanisms by which FGF receptors are activated. Finally, the structure provides a basis for rationalizing the effects of kinase mutations in FGF receptors that lead to developmental disorders in nematodes and humans.

PubMed: 8752212
DOI: 10.1016/S0092-8674(00)80131-2

Experimental method

X-RAY DIFFRACTION (2 Å)