1fq9: Difference between revisions
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{{STRUCTURE_1fq9| PDB=1fq9 | SCENE= }} | |||
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'''CRYSTAL STRUCTURE OF A TERNARY FGF2-FGFR1-HEPARIN COMPLEX''' | '''CRYSTAL STRUCTURE OF A TERNARY FGF2-FGFR1-HEPARIN COMPLEX''' | ||
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[[Category: Yayon, A.]] | [[Category: Yayon, A.]] | ||
[[Category: Yeh, B K.]] | [[Category: Yeh, B K.]] | ||
[[Category: | [[Category: B-trefoil fold]] | ||
[[Category: | [[Category: I-set subgroup within the immunoglobulin superfamily]] | ||
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Revision as of 13:38, 2 May 2008
CRYSTAL STRUCTURE OF A TERNARY FGF2-FGFR1-HEPARIN COMPLEX
Overview
The crystal structure of a dimeric 2:2:2 FGF:FGFR:heparin ternary complex at 3 A resolution has been determined. Within each 1:1 FGF:FGFR complex, heparin makes numerous contacts with both FGF and FGFR, thereby augmenting FGF-FGFR binding. Heparin also interacts with FGFR in the adjoining 1:1 FGF:FGFR complex to promote FGFR dimerization. The 6-O-sulfate group of heparin plays a pivotal role in mediating both interactions. The unexpected stoichiometry of heparin binding in the structure led us to propose a revised model for FGFR dimerization. Biochemical data in support of this model are also presented. This model provides a structural basis for FGFR activation by small molecule heparin analogs and may facilitate the design of heparin mimetics capable of modulating FGF signaling.
About this Structure
1FQ9 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization., Schlessinger J, Plotnikov AN, Ibrahimi OA, Eliseenkova AV, Yeh BK, Yayon A, Linhardt RJ, Mohammadi M, Mol Cell. 2000 Sep;6(3):743-50. PMID:11030354 Page seeded by OCA on Fri May 2 16:38:20 2008
