1x4l: Difference between revisions

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[[Image:1x4l.gif|left|200px]]


{{Structure
==Solution structure of LIM domain in Four and a half LIM domains protein 2==
|PDB= 1x4l |SIZE=350|CAPTION= <scene name='initialview01'>1x4l</scene>
<StructureSection load='1x4l' size='340' side='right'caption='[[1x4l]]' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
<table><tr><td colspan='2'>[[1x4l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X4L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X4L FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
|GENE= FHL2, DRAL, SLIM3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1x4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x4l OCA], [https://pdbe.org/1x4l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x4l RCSB], [https://www.ebi.ac.uk/pdbsum/1x4l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x4l ProSAT], [https://www.topsan.org/Proteins/RSGI/1x4l TOPSAN]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FHL2_HUMAN FHL2_HUMAN] May function as a molecular transmitter linking various signaling pathways to transcriptional regulation. Negatively regulates the transcriptional repressor E4F1 and may function in cell growth. Inhibits the transcriptional activity of FOXO1 and its apoptotic function by enhancing the interaction of FOXO1 with SIRT1 and FOXO1 deacetylation.<ref>PMID:15692560</ref> <ref>PMID:16652157</ref> <ref>PMID:18853468</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/x4/1x4l_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=1x4l ConSurf].
<div style="clear:both"></div>


'''Solution structure of LIM domain in Four and a half LIM domains protein 2'''
==See Also==
 
*[[Muscle LIM protein|Muscle LIM protein]]
 
== References ==
==About this Structure==
<references/>
1X4L 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=1X4L OCA].
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: He, F.]]
[[Category: He F]]
[[Category: Inoue, M.]]
[[Category: Inoue M]]
[[Category: Kigawa, T.]]
[[Category: Kigawa T]]
[[Category: Muto, Y.]]
[[Category: Muto Y]]
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: Shirouzu M]]
[[Category: Shirouzu, M.]]
[[Category: Terada T]]
[[Category: Terada, T.]]
[[Category: Yokoyama S]]
[[Category: Yokoyama, S.]]
[[Category: ZN]]
[[Category: lim domain]]
[[Category: national project on protein structural and functional analyse]]
[[Category: nmr]]
[[Category: nppsfa]]
[[Category: riken structural genomics/proteomics initiative]]
[[Category: rsgi]]
[[Category: structural genomic]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:05:05 2008''

Latest revision as of 16:58, 9 May 2024

Solution structure of LIM domain in Four and a half LIM domains protein 2Solution structure of LIM domain in Four and a half LIM domains protein 2

Structural highlights

1x4l is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

FHL2_HUMAN May function as a molecular transmitter linking various signaling pathways to transcriptional regulation. Negatively regulates the transcriptional repressor E4F1 and may function in cell growth. Inhibits the transcriptional activity of FOXO1 and its apoptotic function by enhancing the interaction of FOXO1 with SIRT1 and FOXO1 deacetylation.[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. ↑ Yang Y, Hou H, Haller EM, Nicosia SV, Bai W. Suppression of FOXO1 activity by FHL2 through SIRT1-mediated deacetylation. EMBO J. 2005 Mar 9;24(5):1021-32. Epub 2005 Feb 3. PMID:15692560 doi:10.1038/sj.emboj.7600570
  2. ↑ Paul C, Lacroix M, Iankova I, Julien E, Schafer BW, Labalette C, Wei Y, Le Cam A, Le Cam L, Sardet C. The LIM-only protein FHL2 is a negative regulator of E4F1. Oncogene. 2006 Sep 7;25(40):5475-84. Epub 2006 May 1. PMID:16652157 doi:http://dx.doi.org/1209567
  3. ↑ Siamakpour-Reihani S, Argiros HJ, Wilmeth LJ, Haas LL, Peterson TA, Johnson DL, Shuster CB, Lyons BA. The cell migration protein Grb7 associates with transcriptional regulator FHL2 in a Grb7 phosphorylation-dependent manner. J Mol Recognit. 2009 Jan-Feb;22(1):9-17. doi: 10.1002/jmr.916. PMID:18853468 doi:http://dx.doi.org/10.1002/jmr.916
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