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1ihk
From Proteopedia
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|PDB= 1ihk |SIZE=350|CAPTION= <scene name='initialview01'>1ihk</scene>, resolution 2.2Å | |PDB= 1ihk |SIZE=350|CAPTION= <scene name='initialview01'>1ihk</scene>, resolution 2.2Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= FGF9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= FGF9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ihk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ihk OCA], [http://www.ebi.ac.uk/pdbsum/1ihk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ihk RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Mohammadi, M.]] | [[Category: Mohammadi, M.]] | ||
[[Category: Plotnikov, A N.]] | [[Category: Plotnikov, A N.]] | ||
| - | [[Category: PO4]] | ||
[[Category: b-trefoil fold]] | [[Category: b-trefoil fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:19:59 2008'' |
Revision as of 18:20, 30 March 2008
| |||||||
| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | FGF9 (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
Page seeded by OCA on Sun Mar 30 21:19:59 2008
