1axm: Difference between revisions

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[[Image:1axm.png|left|200px]]


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==HEPARIN-LINKED BIOLOGICALLY-ACTIVE DIMER OF FIBROBLAST GROWTH FACTOR==
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<StructureSection load='1axm' size='340' side='right'caption='[[1axm]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1axm]] is a 6 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=1AXM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AXM FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IDS:2-O-SULFO-ALPHA-L-IDOPYRANURONIC+ACID'>IDS</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SGN:N,O6-DISULFO-GLUCOSAMINE'>SGN</scene></td></tr>
{{STRUCTURE_1axm|  PDB=1axm  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1axm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1axm OCA], [https://pdbe.org/1axm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1axm RCSB], [https://www.ebi.ac.uk/pdbsum/1axm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1axm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FGF1_HUMAN FGF1_HUMAN] Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as potent mitogen in vitro.<ref>PMID:8663044</ref> <ref>PMID:16597617</ref> <ref>PMID:20145243</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ax/1axm_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1axm ConSurf].
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== Publication Abstract from PubMed ==
The fibroblast growth factors (FGFs) form a large family of structurally related, multifunctional proteins that regulate various biological responses. They mediate cellular functions by binding to transmembrane FGF receptors, which are protein tyrosine kinases. FGF receptors are activated by oligomerization, and both this activation and FGF-stimulated biological responses require heparin-like molecules as well as FGF. Heparins are linear anionic polysaccharide chains; they are typically heterogeneously sulphated on alternating L-iduronic and D-glucosamino sugars, and are nearly ubiquitous in animal tissues as heparan sulphate proteoglycans on cell surfaces and in the extracellular matrix. Although several crystal structures have been described for FGF molecules in complexes with heparin-like sugars, the nature of a biologically active complex has been unknown until now. Here we describe the X-ray crystal structure, at 2.9 A resolution, of a biologically active dimer of human acidic FGF in a complex with a fully sulphated, homogeneous heparin decassacharide. The dimerization of heparin-linked acidic FGF observed here is an elegant mechanism for the modulation of signalling through combinatorial homodimerization and heterodimerization of the 12 known members of the FGF family.


===HEPARIN-LINKED BIOLOGICALLY-ACTIVE DIMER OF FIBROBLAST GROWTH FACTOR===
Structure of a heparin-linked biologically active dimer of fibroblast growth factor.,DiGabriele AD, Lax I, Chen DI, Svahn CM, Jaye M, Schlessinger J, Hendrickson WA Nature. 1998 Jun 25;393(6687):812-7. PMID:9655399<ref>PMID:9655399</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1axm" style="background-color:#fffaf0;"></div>


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==See Also==
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*[[Fibroblast growth factor 3D structures|Fibroblast growth factor 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 9655399 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_9655399}}
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</StructureSection>
==About this Structure==
1AXM 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=1AXM OCA].
 
==Reference==
Structure of a heparin-linked biologically active dimer of fibroblast growth factor., DiGabriele AD, Lax I, Chen DI, Svahn CM, Jaye M, Schlessinger J, Hendrickson WA, Nature. 1998 Jun 25;393(6687):812-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9655399 9655399]
 
X-ray crystal structure of human acidic fibroblast growth factor., Blaber M, DiSalvo J, Thomas KA, Biochemistry. 1996 Feb 20;35(7):2086-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8652550 8652550]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Chen, D I.]]
[[Category: Chen DI]]
[[Category: DiGabriele, A D.]]
[[Category: DiGabriele AD]]
[[Category: Hendrickson, W A.]]
[[Category: Hendrickson WA]]
[[Category: Jaye, M.]]
[[Category: Jaye M]]
[[Category: Lax, I.]]
[[Category: Lax I]]
[[Category: Schlessinger, J.]]
[[Category: Schlessinger J]]
[[Category: Svahn, C M.]]
[[Category: Svahn CM]]
[[Category: Heparin decasaccharide]]
[[Category: Human acidic fibroblast growth factor]]
 
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