Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1DJS

LIGAND-BINDING PORTION OF FIBROBLAST GROWTH FACTOR RECEPTOR 2 IN COMPLEX WITH FGF1

Summary for 1DJS
Entry DOI10.2210/pdb1djs/pdb
DescriptorPROTEIN (FIBROBLAST GROWTH FACTOR RECEPTOR 2), PROTEIN (FIBROBLAST GROWTH FACTOR 1), SULFATE ION, ... (4 entities in total)
Functional Keywordsfgfr, fgf, immunoglobulin, immune system, hormone-growth factor-receptor complex, hormone/growth factor/receptor
Biological sourceHomo sapiens (human)
More
Cellular locationCell membrane; Single-pass type I membrane protein. Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 3: Cell membrane; Single-pass type I membrane protein. Isoform 14: Secreted. Isoform 19: Secreted: P21802
Secreted: P05230
Total number of polymer chains2
Total formula weight40499.60
Authors
Stauber, D.J.,Digabriele, A.D.,Hendrickson, W.A. (deposition date: 1999-12-03, release date: 2000-01-12, Last modification date: 2024-11-06)
Primary citationStauber, D.J.,DiGabriele, A.D.,Hendrickson, W.A.
Structural interactions of fibroblast growth factor receptor with its ligands.
Proc.Natl.Acad.Sci.USA, 97:49-54, 2000
Cited by
PubMed Abstract: 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.
PubMed: 10618369
DOI: 10.1073/pnas.97.1.49
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

237423

PDB entries from 2025-06-11

PDB statisticsPDBj update infoContact PDBjnumon