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| {{STRUCTURE_1g82| PDB=1g82 | SCENE= }} | | {{STRUCTURE_1g82| PDB=1g82 | SCENE= }} |
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| '''STRUCTURE OF FIBROBLAST GROWTH FACTOR 9'''
| | ===STRUCTURE OF FIBROBLAST GROWTH FACTOR 9=== |
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| ==Overview==
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| Fibroblast growth factors (FGFs) constitute a family of at least 20 structurally related heparin-binding polypeptides active in regulating cell growth, survival, differentiation and migration. FGF9, originally discovered as a glia-activating factor, shares 30% sequence identity with other FGFs and has a unique spectrum of target-cell specificity. FGF9 crystallized in the tetragonal space group I4(1), with unit-cell parameters a = b = 151.9, c = 117.2 A. The structure of the glycosylated protein has been refined to an R value of 21.0% with R(free) = 24.8%) at 2.6 A resolution. The four molecules in the asymmetric unit are arranged in two non-crystallographic dimers, with the dimer interface composed partly of residues from N- and C-terminal extensions from the FGF core structure. Most of the receptor-binding residues identified in FGF1- and FGF2-receptor complexes are buried in the dimer interface, with the beta8-beta9 loop stabilized in a particular conformation by an intramolecular hydrogen-bonding network. The potential heparin-binding sites are in a pattern distinct from FGF1 and FGF2. The carbohydrate moiety attached at Asn79 has no structural influence.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11223514}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11223514 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11223514}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Yayon, A.]] | | [[Category: Yayon, A.]] |
| [[Category: Fibroblast growth factor]] | | [[Category: Fibroblast growth factor]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:15:29 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:51:40 2008'' |
