3crh: Difference between revisions

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New page: '''Unreleased structure''' The entry 3crh is ON HOLD until Paper Publication Authors: Meher, A.K., Honjo, E., Kuroki, R., Lee, J., Somasundaram, T., Blaber, M. Description: Crystal str...
 
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'''Unreleased structure'''


The entry 3crh is ON HOLD  until Paper Publication
==Crystal structure of human fibroblast growth factor-1 with mutations Glu81Ser and Lys101Ala==
<StructureSection load='3crh' size='340' side='right'caption='[[3crh]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3crh]] is a 2 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=3CRH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CRH 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]] 2.15&#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=3crh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3crh OCA], [https://pdbe.org/3crh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3crh RCSB], [https://www.ebi.ac.uk/pdbsum/3crh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3crh 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/cr/3crh_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=3crh ConSurf].
<div style="clear:both"></div>


Authors: Meher, A.K., Honjo, E., Kuroki, R., Lee, J., Somasundaram, T., Blaber, M.
==See Also==
 
*[[Fibroblast growth factor 3D structures|Fibroblast growth factor 3D structures]]
Description: Crystal structure of human fibroblast growth factor-1 with mutations Glu81Ser and Lys101Ala
== References ==
 
<references/>
 
__TOC__
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 11 09:33:42 2008''
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Blaber M]]
[[Category: Honjo E]]
[[Category: Kuroki R]]
[[Category: Lee J]]
[[Category: Meher AK]]
[[Category: Somasundaram T]]

Latest revision as of 12:37, 21 February 2024

Crystal structure of human fibroblast growth factor-1 with mutations Glu81Ser and Lys101AlaCrystal structure of human fibroblast growth factor-1 with mutations Glu81Ser and Lys101Ala

Structural highlights

3crh is a 2 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 2.15Å
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

3crh, resolution 2.15Å

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