1evt: Difference between revisions

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New page: left|200px<br /> <applet load="1evt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1evt, resolution 2.80Å" /> '''CRYSTAL STRUCTURE O...
 
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[[Image:1evt.gif|left|200px]]<br />
<applet load="1evt" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1evt, resolution 2.80&Aring;" />
'''CRYSTAL STRUCTURE OF FGF1 IN COMPLEX WITH THE EXTRACELLULAR LIGAND BINDING DOMAIN OF FGF RECEPTOR 1 (FGFR1)'''<br />


==Overview==
==CRYSTAL STRUCTURE OF FGF1 IN COMPLEX WITH THE EXTRACELLULAR LIGAND BINDING DOMAIN OF FGF RECEPTOR 1 (FGFR1)==
To elucidate the structural determinants governing specificity in, fibroblast growth factor (FGF) signaling, we have determined the crystal, structures of FGF1 and FGF2 complexed with the ligand binding domains, (immunoglobulin-like domains 2 [D2] and 3 [D3]) of FGF receptor 1 (FGFR1), and FGFR2, respectively. Highly conserved FGF-D2 and FGF-linker (between, D2-D3) interfaces define a general binding site for all FGF-FGFR, complexes. Specificity is achieved through interactions between the, N-terminal and central regions of FGFs and two loop regions in D3 that are, subject to alternative splicing. These structures provide a molecular, basis for FGF1 as a universal FGFR ligand and for modulation of FGF-FGFR, specificity through primary sequence variations and alternative splicing.
<StructureSection load='1evt' size='340' side='right'caption='[[1evt]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1evt]] is a 4 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=1EVT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EVT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1evt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1evt OCA], [https://pdbe.org/1evt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1evt RCSB], [https://www.ebi.ac.uk/pdbsum/1evt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1evt 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/ev/1evt_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1evt ConSurf].
<div style="clear:both"></div>


==Disease==
==See Also==
Known diseases associated with this structure: Aplasia of lacrimal and salivary glands OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=602115 602115]], Atopic dermatitis, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=135940 135940]], Ichthyosis vulgaris OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=135940 135940]], Jackson-Weiss syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=136350 136350]], Kallmann syndrome 2 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=136350 136350]], LADD syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=602115 602115]], Pfeiffer syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=136350 136350]]
*[[Fibroblast growth factor 3D structures|Fibroblast growth factor 3D structures]]
 
*[[Fibroblast growth factor receptor|Fibroblast growth factor receptor]]
==About this Structure==
*[[Fibroblast growth factor receptor 3D receptor|Fibroblast growth factor receptor 3D receptor]]
1EVT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EVT OCA].
== References ==
 
<references/>
==Reference==
__TOC__
Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity., Plotnikov AN, Hubbard SR, Schlessinger J, Mohammadi M, Cell. 2000 May 12;101(4):413-24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10830168 10830168]
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Hubbard, S.R.]]
[[Category: Hubbard SR]]
[[Category: Mohammadi, M.]]
[[Category: Mohammadi M]]
[[Category: Plotnikov, A.N.]]
[[Category: Plotnikov AN]]
[[Category: Schlessinger, J.]]
[[Category: Schlessinger J]]
[[Category: SO4]]
[[Category: b-trefoil fold]]
[[Category: immunoglobulin (ig) like domains belonging to the i-set subgroup within ig-like domains]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:47:04 2007''

Latest revision as of 13:07, 20 March 2024

CRYSTAL STRUCTURE OF FGF1 IN COMPLEX WITH THE EXTRACELLULAR LIGAND BINDING DOMAIN OF FGF RECEPTOR 1 (FGFR1)CRYSTAL STRUCTURE OF FGF1 IN COMPLEX WITH THE EXTRACELLULAR LIGAND BINDING DOMAIN OF FGF RECEPTOR 1 (FGFR1)

Structural highlights

1evt is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2] [3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Ornitz DM, Xu J, Colvin JS, McEwen DG, MacArthur CA, Coulier F, Gao G, Goldfarb M. Receptor specificity of the fibroblast growth factor family. J Biol Chem. 1996 Jun 21;271(25):15292-7. PMID:8663044
  2. ↑ Zhang X, Ibrahimi OA, Olsen SK, Umemori H, Mohammadi M, Ornitz DM. Receptor specificity of the fibroblast growth factor family. The complete mammalian FGF family. J Biol Chem. 2006 Jun 9;281(23):15694-700. Epub 2006 Apr 4. PMID:16597617 doi:10.1074/jbc.M601252200
  3. ↑ Fernandez IS, Cuevas P, Angulo J, Lopez-Navajas P, Canales-Mayordomo A, Gonzalez-Corrochano R, Lozano RM, Valverde S, Jimenez-Barbero J, Romero A, Gimenez-Gallego G. Gentisic acid, a compound associated with plant defense and a metabolite of aspirin, heads a new class of in vivo fibroblast growth factor inhibitors. J Biol Chem. 2010 Apr 9;285(15):11714-29. Epub 2010 Feb 9. PMID:20145243 doi:10.1074/jbc.M109.064618

1evt, resolution 2.80Å

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