1g82: Difference between revisions
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[[Image:1g82.gif|left|200px]] | [[Image:1g82.gif|left|200px]] | ||
'''STRUCTURE OF FIBROBLAST GROWTH FACTOR 9''' | {{Structure | ||
|PDB= 1g82 |SIZE=350|CAPTION= <scene name='initialview01'>1g82</scene>, resolution 2.6Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''STRUCTURE OF FIBROBLAST GROWTH FACTOR 9''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1G82 is a [ | 1G82 is a [[Single protein]] structure of sequence 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=1G82 OCA]. | ||
==Reference== | ==Reference== | ||
Structure of fibroblast growth factor 9 shows a symmetric dimer with unique receptor- and heparin-binding interfaces., Hecht HJ, Adar R, Hofmann B, Bogin O, Weich H, Yayon A, Acta Crystallogr D Biol Crystallogr. 2001 Mar;57(Pt 3):378-84. PMID:[http:// | Structure of fibroblast growth factor 9 shows a symmetric dimer with unique receptor- and heparin-binding interfaces., Hecht HJ, Adar R, Hofmann B, Bogin O, Weich H, Yayon A, Acta Crystallogr D Biol Crystallogr. 2001 Mar;57(Pt 3):378-84. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11223514 11223514] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: fibroblast growth factor]] | [[Category: fibroblast growth factor]] | ||
''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 11:19:29 2008'' | ||
Revision as of 09:19, 20 March 2008
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| 1g82, resolution 2.6Å | |||||||||||||
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| Ligands: | NAG and SO4 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
STRUCTURE OF FIBROBLAST GROWTH FACTOR 9
Overview
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.
About this Structure
1G82 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of fibroblast growth factor 9 shows a symmetric dimer with unique receptor- and heparin-binding interfaces., Hecht HJ, Adar R, Hofmann B, Bogin O, Weich H, Yayon A, Acta Crystallogr D Biol Crystallogr. 2001 Mar;57(Pt 3):378-84. PMID:11223514
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