1ihk
From Proteopedia
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- | [[Image:1ihk.jpg|left|200px]] | + | [[Image:1ihk.jpg|left|200px]] |
- | + | ||
- | '''CRYSTAL STRUCTURE OF FIBROBLAST GROWTH FACTOR 9 (FGF9)''' | + | {{Structure |
+ | |PDB= 1ihk |SIZE=350|CAPTION= <scene name='initialview01'>1ihk</scene>, resolution 2.2Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= FGF9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
+ | }} | ||
+ | |||
+ | '''CRYSTAL STRUCTURE OF FIBROBLAST GROWTH FACTOR 9 (FGF9)''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1IHK is a [ | + | 1IHK 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=1IHK OCA]. |
==Reference== | ==Reference== | ||
- | Crystal structure of fibroblast growth factor 9 reveals regions implicated in dimerization and autoinhibition., Plotnikov AN, Eliseenkova AV, Ibrahimi OA, Shriver Z, Sasisekharan R, Lemmon MA, Mohammadi M, J Biol Chem. 2001 Feb 9;276(6):4322-9. Epub 2000 Nov 1. PMID:[http:// | + | Crystal structure of fibroblast growth factor 9 reveals regions implicated in dimerization and autoinhibition., Plotnikov AN, Eliseenkova AV, Ibrahimi OA, Shriver Z, Sasisekharan R, Lemmon MA, Mohammadi M, J Biol Chem. 2001 Feb 9;276(6):4322-9. Epub 2000 Nov 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11060292 11060292] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: b-trefoil fold]] | [[Category: b-trefoil fold]] | ||
- | ''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 11:50:32 2008'' |
Revision as of 09:50, 20 March 2008
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, resolution 2.2Å | |||||||
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Ligands: | |||||||
Gene: | FGF9 (Homo sapiens) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
CRYSTAL STRUCTURE OF FIBROBLAST GROWTH FACTOR 9 (FGF9)
Overview
Fibroblast growth factors (FGFs) constitute a large family of heparin-binding growth factors with diverse biological activities. FGF9 was originally described as glia-activating factor and is expressed in the nervous system as a potent mitogen for glia cells. Unlike most FGFs, FGF9 forms dimers in solution with a K(d) of 680 nm. To elucidate the molecular mechanism of FGF9 dimerization, the crystal structure of FGF9 was determined at 2.2 A resolution. FGF9 adopts a beta-trefoil fold similar to other FGFs. However, unlike other FGFs, the N- and C-terminal regions outside the beta-trefoil core in FGF9 are ordered and involved in the formation of a 2-fold crystallographic dimer. A significant surface area (>2000 A(2)) is buried in the dimer interface that occludes a major receptor binding site of FGF9. Thus, we propose an autoinhibitory mechanism for FGF9 that is dependent on sequences outside of the beta-trefoil core. Moreover, a model is presented providing a molecular basis for the preferential affinity of FGF9 toward FGFR3.
About this Structure
1IHK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of fibroblast growth factor 9 reveals regions implicated in dimerization and autoinhibition., Plotnikov AN, Eliseenkova AV, Ibrahimi OA, Shriver Z, Sasisekharan R, Lemmon MA, Mohammadi M, J Biol Chem. 2001 Feb 9;276(6):4322-9. Epub 2000 Nov 1. PMID:11060292
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