2biv: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: left|200px<br /> <applet load="2biv" size="450" color="white" frame="true" align="right" spinBox="true" caption="2biv, resolution 1.70Å" /> '''CRYSTAL STRUCTURE O...
 
OCA (talk | contribs)
No edit summary
 
(22 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2biv.gif|left|200px]]<br />
<applet load="2biv" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2biv, resolution 1.70&Aring;" />
'''CRYSTAL STRUCTURE OF THE WILD-TYPE MBT DOMAINS OF HUMAN SCML2'''<br />


==About this Structure==
==Crystal structure of the wild-type MBT domains of Human SCML2==
2BIV is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with IOD and NA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BIV OCA]].  
<StructureSection load='2biv' size='340' side='right'caption='[[2biv]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2biv]] is a 3 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=2BIV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BIV 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]] 1.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=2biv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2biv OCA], [https://pdbe.org/2biv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2biv RCSB], [https://www.ebi.ac.uk/pdbsum/2biv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2biv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SCML2_HUMAN SCML2_HUMAN] Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development (By similarity).
== 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/bi/2biv_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=2biv ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
SCML2 (sex comb on midleg-like 2) is a constituent of the Polycomb repressive complex 1, a large multiprotein assembly required for the repression of developmental control genes. It contains two MBT (malignant brain tumor) repeats; the MBT is a protein module structurally similar to domains that bind to methylated histones. We have used NMR spectroscopy to examine the binding specificity of these repeats. Our data show that they preferentially bind histone peptides monomethylated at lysine residues with no apparent sequence specificity. The crystal structure of the complex between the protein and monomethyllysine reveals that the modified amino acid binds to an aromatic rich pocket at one end of the beta-barrel of the second repeat.
 
The malignant brain tumor repeats of human SCML2 bind to peptides containing monomethylated lysine.,Santiveri CM, Lechtenberg BC, Allen MD, Sathyamurthy A, Jaulent AM, Freund SM, Bycroft M J Mol Biol. 2008 Oct 24;382(5):1107-12. Epub 2008 Aug 3. PMID:18706910<ref>PMID:18706910</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2biv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Allen, M.D.]]
[[Category: Allen MD]]
[[Category: Bycroft, M.]]
[[Category: Bycroft M]]
[[Category: Sait, F.]]
[[Category: Sait F]]
[[Category: Santiveri, C.M.]]
[[Category: Santiveri CM]]
[[Category: IOD]]
[[Category: NA]]
[[Category: malignant brain tumor]]
[[Category: mbt]]
[[Category: scml2]]
[[Category: transcription factor]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 21:49:05 2007''

Latest revision as of 13:39, 13 December 2023

Crystal structure of the wild-type MBT domains of Human SCML2

2biv, resolution 1.70Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA