1ihk
From Proteopedia
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==CRYSTAL STRUCTURE OF FIBROBLAST GROWTH FACTOR 9 (FGF9)== | ==CRYSTAL STRUCTURE OF FIBROBLAST GROWTH FACTOR 9 (FGF9)== | ||
| - | <StructureSection load='1ihk' size='340' side='right' caption='[[1ihk]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='1ihk' size='340' side='right'caption='[[1ihk]], [[Resolution|resolution]] 2.20Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1ihk]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1ihk]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IHK FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ihk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ihk OCA], [https://pdbe.org/1ihk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ihk RCSB], [https://www.ebi.ac.uk/pdbsum/1ihk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ihk ProSAT]</span></td></tr> |
</table> | </table> | ||
== Disease == | == Disease == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/FGF9_HUMAN FGF9_HUMAN] Defects in FGF9 are the cause of multiple synostoses syndrome type 3 (SYNS3) [MIM:[https://omim.org/entry/612961 612961]. Multiple synostoses syndrome is an autosomal dominant condition characterized by progressive joint fusions of the fingers, wrists, ankles and cervical spine, characteristic facies and progressive conductive deafness.<ref>PMID:19589401</ref> |
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/FGF9_HUMAN FGF9_HUMAN] Plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. May have a role in glial cell growth and differentiation during development, gliosis during repair and regeneration of brain tissue after damage, differentiation and survival of neuronal cells, and growth stimulation of glial tumors.<ref>PMID:8663044</ref> <ref>PMID:16597617</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ihk ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ihk ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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. | ||
| - | + | ==See Also== | |
| - | + | *[[Fibroblast growth factor 3D structures|Fibroblast growth factor 3D structures]] | |
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== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Eliseenkova AV]] |
| - | [[Category: | + | [[Category: Ibrahimi OA]] |
| - | [[Category: | + | [[Category: Lemmon MA]] |
| - | [[Category: | + | [[Category: Mohammadi M]] |
| - | [[Category: | + | [[Category: Plotnikov AN]] |
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Current revision
CRYSTAL STRUCTURE OF FIBROBLAST GROWTH FACTOR 9 (FGF9)
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