Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin

Nature

Volumn 407, Issue 6807, 2000, Pages 1029-1034

  Pellegrini, Luca ^a   Burke, David F ^a   Von Delft, Frank ^a   Mulloy, Barbara ^b   Blundell, Tom L ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b NATIONAL INSTITUTE FOR BIOLOGICAL STANDARDS AND CONTROL   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

FIBROBLAST GROWTH FACTOR RECEPTOR; HEPARIN;

ARTICLE; BINDING AFFINITY; COMPLEX FORMATION; CRYSTAL STRUCTURE; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION;

AMINO ACID SEQUENCE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; FIBROBLAST GROWTH FACTOR 1; FIBROBLAST GROWTH FACTOR 2; HEPARIN; HUMANS; LIGANDS; MACROMOLECULAR SUBSTANCES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RECEPTOR PROTEIN-TYROSINE KINASES; RECEPTOR, FIBROBLAST GROWTH FACTOR, TYPE 2; RECEPTORS, FIBROBLAST GROWTH FACTOR; RECOMBINANT PROTEINS;

EID: 0034718796     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/35039551     Document Type: Article

References (30)

1. Fibroblast growth factors and their receptors
2. Structural and functional diversity in the FGF receptor multigene family
3. Requirement of heparan sulfate for bFGF-mediated fibroblast growth and myoblast differentiation
4. Heparin-induced oligomerization of FGF molecules is responsible for FGF receptor dimerization, activation and cell proliferation
5. Heparan sulfate proteoglycans are essential for FGF receptor signaling during Drosophila embryonic development
6. Heparin structure and interactions with basic fibroblast growth factor
7. Structure of a heparin-linked biologically active dimer of fibroblast growth factor
8. Structural basis for FGF receptor dimerization and activation
9. Structural Interactions of fibroblast growth factor receptor with its ligands
10. Three-dimensional structure of acidic and basic fibroblast growth factor
11. Energetic characterization of the basic fibroblast growth factor-heparin interaction: Identification of the heparin binding domain
12. Identification and concerted function of two receptor binding surfaces on basic fibroblast growth factor required for mitogenesis
13. An essential heparin-binding domain in the fibroblast growth factor receptor kinase
14. Activating and inhibitory heparin sequences for FGF-2 (basic FGF). Distinct requirements for FGF-1, FGF-2, and FGF-4
15. Heparin is required for cell-free binding of basic fibroblast growth factor to a soluble receptor and for mitogenesis in whole cells
16. Importance of size, sulfation, and anticoagulant activity in the potentiation of acidic fibroblast growth factor by heparin
17. Ligand-specific structural domains in the fibroblast growth factor receptor
18. Analysis of high-affinity binding determinants in the receptor binding epitope of basic fibroblast growth factor
19. Glu-96 of basic fibroblast growth factor is essential for high affinity receptor binding. Identification by structure-based site-directed mutagenesis
20. Convergence of integrin and growth factor receptor signaling pathways within the focal adhesion complex
21. Genotype-phenotype correlation for nucleotide substitutions in the IgII-IgIII linker of FGFR2
22. Side-chain effects on peptidyl-prolyl cis/trans isomerisation
23. High-performance liquid chromatographic separation of heparin-derived oligosaccharides
24. Processing of X-ray diffraction data collected in oscillation mode
25. SHELXL: High resolution refinement
26. Maximum-likelihood heavy-atom parameter refinement in the MIR and MAD methods
27. Methods used in the structure determination of bovine mitochondrial F1 ATPase
28. N.m.r. and molecular-modelling studies of the solution conformation of heparin
29. Crystallography and NMR system: A new software suite for macromolecular structure determination
30. Improved methods for binding protein models in electron-density maps and the location of errors in these models