1cvs | pdb_00001cvs
CRYSTAL STRUCTURE OF A DIMERIC FGF2-FGFR1 COMPLEX
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| 1cvs, resolution 2.80Å | |||||||||||||
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| Ligands: | SO4 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
The crystal structure of FGF2 bound to a naturally occurring variant of FGF receptor 1 (FGFR1) consisting of immunoglobulin-like domains 2 (D2) and 3 (D3) has been determined at 2.8 A resolution. Two FGF2:FGFR1 complexes form a 2-fold symmetric dimer. Within each complex, FGF2 interacts extensively with D2 and D3 as well as with the linker between the two domains. The dimer is stabilized by interactions between FGF2 and D2 of the adjoining complex and by a direct interaction between D2 of each receptor. A positively charged canyon formed by a cluster of exposed basic residues likely represents the heparin-binding site. A general model for FGF- and heparin-induced FGFR dimerization is inferred from the crystal structure, unifying a wealth of biochemical data.
Disease
Known diseases associated with this structure: Atopic dermatitis, susceptibility to OMIM:[135940], Hypophosphatemic rickets, autosomal dominant OMIM:[605380], Ichthyosis vulgaris OMIM:[135940], Jackson-Weiss syndrome OMIM:[136350], Kallmann syndrome 2 OMIM:[136350], Osteomalacia, tumor-induced OMIM:[605380], Pfeiffer syndrome OMIM:[136350], Tumoral calcinosis, hyperphosphatemic, familial OMIM:[605380]
About this Structure
1CVS is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis for FGF receptor dimerization and activation., Plotnikov AN, Schlessinger J, Hubbard SR, Mohammadi M, Cell. 1999 Sep 3;98(5):641-50. PMID:10490103
Page seeded by OCA on Thu Mar 20 10:29:34 2008
