1fq9: Difference between revisions
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[[Image:1fq9.jpg|left|200px]] | [[Image:1fq9.jpg|left|200px]] | ||
'''CRYSTAL STRUCTURE OF A TERNARY FGF2-FGFR1-HEPARIN COMPLEX''' | {{Structure | ||
|PDB= 1fq9 |SIZE=350|CAPTION= <scene name='initialview01'>1fq9</scene>, resolution 3.0Å | |||
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|LIGAND= | |||
|ACTIVITY= | |||
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'''CRYSTAL STRUCTURE OF A TERNARY FGF2-FGFR1-HEPARIN COMPLEX''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1FQ9 is a [ | 1FQ9 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQ9 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11030354 11030354] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: i-set subgroup within the immunoglobulin superfamily]] | [[Category: i-set subgroup within the immunoglobulin superfamily]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:12:33 2008'' | ||
Revision as of 09:12, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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.
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
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 Thu Mar 20 11:12:33 2008
