TI  - Structural interactions of fibroblast growth factor receptor with its
      ligands.
PG  - 49-54
AB  -  Fibroblast growth factors (FGFs)  effect cellular responses by binding to
       FGF receptors (FGFRs) .  FGF  bound to extracellular domains on the  FGFR  in
      the presence of heparin activates the cytoplasmic receptor tyrosine kinase
      through autophosphorylation. We have crystallized a complex between  human
      <prot>FGF1</prot>  and a two-domain extracellular fragment of human <prot>FGFR2</prot> . The crystal
      structure, determined by multiwavelength anomalous diffraction analysis of
      the selenomethionyl protein, is a dimeric assemblage of 1:1
      ligand:receptor complexes.  FGF  is bound at the junction between the two
      domains of one  FGFR , and two such units are associated through
      receptor:receptor and secondary ligand:receptor interfaces. Sulfate ion
      positions appear to mark the course of heparin binding between FGF
      molecules through a basic region on receptor D2 domains. This dimeric
      assemblage provides a structural mechanism for FGF signal transduction.
AD  - Department of Biochemistry, Columbia University, New York, NY 10032, USA.
