1ihk: Difference between revisions

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[[Image:1ihk.jpg|left|200px]]
[[Image:1ihk.jpg|left|200px]]


{{Structure
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|SITE=
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|GENE= FGF9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
{{STRUCTURE_1ihk| PDB=1ihk  | SCENE= }}  
|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>
}}


'''CRYSTAL STRUCTURE OF FIBROBLAST GROWTH FACTOR 9 (FGF9)'''
'''CRYSTAL STRUCTURE OF FIBROBLAST GROWTH FACTOR 9 (FGF9)'''
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[[Category: Mohammadi, M.]]
[[Category: Mohammadi, M.]]
[[Category: Plotnikov, A N.]]
[[Category: Plotnikov, A N.]]
[[Category: b-trefoil fold]]
[[Category: B-trefoil fold]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 20:00:28 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:19:59 2008''

Revision as of 20:00, 2 May 2008

File:1ihk.jpg

Template:STRUCTURE 1ihk

CRYSTAL STRUCTURE OF FIBROBLAST GROWTH FACTOR 9 (FGF9)


OverviewOverview

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 StructureAbout this Structure

1IHK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

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 Fri May 2 20:00:28 2008

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