1g82
From Proteopedia
(New page: 200px<br /><applet load="1g82" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g82, resolution 2.6Å" /> '''STRUCTURE OF FIBROBLA...) |
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| - | [[Image:1g82.gif|left|200px]]<br /><applet load="1g82" size=" | + | [[Image:1g82.gif|left|200px]]<br /><applet load="1g82" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1g82, resolution 2.6Å" /> | caption="1g82, resolution 2.6Å" /> | ||
'''STRUCTURE OF FIBROBLAST GROWTH FACTOR 9'''<br /> | '''STRUCTURE OF FIBROBLAST GROWTH FACTOR 9'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Fibroblast growth factors (FGFs) constitute a family of at least 20 | + | 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== | ==About this Structure== | ||
| - | 1G82 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1G82 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G82 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Adar, R.]] | [[Category: Adar, R.]] | ||
[[Category: Bogin, O.]] | [[Category: Bogin, O.]] | ||
| - | [[Category: Hecht, H | + | [[Category: Hecht, H J.]] |
[[Category: Hofmann, B.]] | [[Category: Hofmann, B.]] | ||
[[Category: Weich, H.]] | [[Category: Weich, H.]] | ||
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[[Category: fibroblast growth factor]] | [[Category: fibroblast growth factor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:47:13 2008'' |
Revision as of 10:47, 21 February 2008
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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 with and as ligands. 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
Page seeded by OCA on Thu Feb 21 12:47:13 2008
Categories: Homo sapiens | Single protein | Adar, R. | Bogin, O. | Hecht, H J. | Hofmann, B. | Weich, H. | Yayon, A. | NAG | SO4 | Fibroblast growth factor
