PMID- 10618369
OWN - NLM
STAT- MEDLINE
DCOM- 20000210
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 97
IP  - 1
DP  - 2000 Jan 4
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 FGF1 and a
      two-domain extracellular fragment of human FGFR2. 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.
FAU - Stauber, D J
AU  - Stauber DJ
AD  - Department of Biochemistry, Columbia University, New York, NY 10032, USA.
FAU - DiGabriele, A D
AU  - DiGabriele AD
FAU - Hendrickson, W A
AU  - Hendrickson WA
LA  - eng
SI  - PDB/1DJS
GR  - R37 GM034102/GM/NIGMS NIH HHS/United States
GR  - R01 GM034102/GM/NIGMS NIH HHS/United States
GR  - GM34102/GM/NIGMS NIH HHS/United States
GR  - T32 EY007105/EY/NEI NIH HHS/United States
GR  - EY07105/EY/NEI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Ligands)
RN  - 0 (Proteins)
RN  - 0 (Receptors, Fibroblast Growth Factor)
RN  - 0 (Selenoproteins)
RN  - 103107-01-3 (Fibroblast Growth Factor 2)
RN  - 104781-85-3 (Fibroblast Growth Factor 1)
RN  - 9005-49-6 (Heparin)
RN  - 964MRK2PEL (Selenomethionine)
RN  - EC 2.7.10.1 (FGFR2 protein, human)
RN  - EC 2.7.10.1 (Receptor Protein-Tyrosine Kinases)
RN  - EC 2.7.10.1 (Receptor, Fibroblast Growth Factor, Type 2)
SB  - IM
MH  - Amino Acid Sequence
MH  - Binding Sites
MH  - Crystallization
MH  - Databases, Factual
MH  - Dimerization
MH  - Fibroblast Growth Factor 1
MH  - Fibroblast Growth Factor 2/*chemistry
MH  - Heparin/chemistry
MH  - Humans
MH  - Ligands
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Protein Binding
MH  - Protein Conformation
MH  - Proteins/chemistry
MH  - Receptor Protein-Tyrosine Kinases/*chemistry
MH  - Receptor, Fibroblast Growth Factor, Type 2
MH  - Receptors, Fibroblast Growth Factor/*chemistry
MH  - Selenomethionine/chemistry
MH  - Selenoproteins
MH  - Sequence Alignment
MH  - Signal Transduction
MH  - X-Ray Diffraction
PMC - PMC26614
EDAT- 2000/01/05 00:00
MHDA- 2000/01/05 00:01
CRDT- 2000/01/05 00:00
PHST- 2000/01/05 00:00 [pubmed]
PHST- 2000/01/05 00:01 [medline]
PHST- 2000/01/05 00:00 [entrez]
AID - 10.1073/pnas.97.1.49 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 2000 Jan 4;97(1):49-54. doi: 10.1073/pnas.97.1.49.