1CVS

CRYSTAL STRUCTURE OF A DIMERIC FGF2-FGFR1 COMPLEX

Summary for 1CVS

• Entry DOI: 10.2210/pdb1cvs/pdb
• Descriptor: FIBROBLAST GROWTH FACTOR 2, FIBROBLAST GROWTH FACTOR RECEPTOR 1, SULFATE ION (3 entities in total)
• Functional Keywords: fgf, fgfr, immunoglobulin-like, signal transduction, dimerization, growth factor-growth factor receptor complex, growth factor/growth factor receptor
• Biological source: Homo sapiens (human); More
• Cellular location: Membrane; Single-pass type I membrane protein: P11362
• Total number of polymer chains: 4
• Total formula weight: 81154.54

Authors

Plotnikov, A.N.,Schlessinger, J.,Hubbard, S.R.,Mohammadi, M. (deposition date: 1999-08-24, release date: 2000-01-28, Last modification date: 2024-04-03)

Primary citation

Plotnikov, A.N.,Schlessinger, J.,Hubbard, S.R.,Mohammadi, M.
Structural basis for FGF receptor dimerization and activation.
Cell(Cambridge,Mass.), 98:641-650, 1999

PubMed Abstract: The crystal structure of FGF2 bound to a naturally occurring variant of FGF receptor 1 (FGFR1) consisting of immunoglobulin-like domains 2 (D2) and 3 (D3) has been determined at 2.8 A resolution. Two FGF2:FGFR1 complexes form a 2-fold symmetric dimer. Within each complex, FGF2 interacts extensively with D2 and D3 as well as with the linker between the two domains. The dimer is stabilized by interactions between FGF2 and D2 of the adjoining complex and by a direct interaction between D2 of each receptor. A positively charged canyon formed by a cluster of exposed basic residues likely represents the heparin-binding site. A general model for FGF- and heparin-induced FGFR dimerization is inferred from the crystal structure, unifying a wealth of biochemical data.

PubMed: 10490103
DOI: 10.1016/S0092-8674(00)80051-3

Experimental method

X-RAY DIFFRACTION (2.8 Å)