1cvs: Difference between revisions
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'''CRYSTAL STRUCTURE OF A DIMERIC FGF2-FGFR1 COMPLEX''' | '''CRYSTAL STRUCTURE OF A DIMERIC FGF2-FGFR1 COMPLEX''' | ||
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[[Category: Plotnikov, A N.]] | [[Category: Plotnikov, A N.]] | ||
[[Category: Schlessinger, J.]] | [[Category: Schlessinger, J.]] | ||
[[Category: | [[Category: Dimerization]] | ||
[[Category: | [[Category: Fgf]] | ||
[[Category: | [[Category: Fgfr]] | ||
[[Category: | [[Category: Immunoglobulin-like]] | ||
[[Category: | [[Category: Signal transduction]] | ||
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Revision as of 13:09, 2 May 2008
CRYSTAL STRUCTURE OF A DIMERIC FGF2-FGFR1 COMPLEX
OverviewOverview
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.
About this StructureAbout this Structure
1CVS is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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 Fri May 2 13:09:49 2008