1DJS
LIGAND-BINDING PORTION OF FIBROBLAST GROWTH FACTOR RECEPTOR 2 IN COMPLEX WITH FGF1
Summary for 1DJS
Entry DOI | 10.2210/pdb1djs/pdb |
Descriptor | PROTEIN (FIBROBLAST GROWTH FACTOR RECEPTOR 2), PROTEIN (FIBROBLAST GROWTH FACTOR 1), SULFATE ION, ... (4 entities in total) |
Functional Keywords | fgfr, fgf, immunoglobulin, immune system, hormone-growth factor-receptor complex, hormone/growth factor/receptor |
Biological source | Homo sapiens (human) More |
Cellular location | Cell 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 chains | 2 |
Total formula weight | 40499.60 |
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 citation | Stauber, 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: 10618369DOI: 10.1073/pnas.97.1.49 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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