1ihk: Difference between revisions

Revision as of 12:12, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1ihk.png

Template:STRUCTURE 1ihk

CRYSTAL STRUCTURE OF FIBROBLAST GROWTH FACTOR 9 (FGF9)CRYSTAL STRUCTURE OF FIBROBLAST GROWTH FACTOR 9 (FGF9)

Template:ABSTRACT PUBMED 11060292

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 Tue Jul 1 12:12:27 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1ihk.jpg|left|200px]]
+{{Seed}}
+[[Image:1ihk.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1ihk|  PDB=1ihk  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF FIBROBLAST GROWTH FACTOR 9 (FGF9)'''
+===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 (&gt;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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11060292}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11060292 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11060292}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Plotnikov, A N.]]
 [[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 Tue Jul  1 12:12:27 2008''