4lce
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4lce]] is a 1 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=4LCE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LCE FirstGlance]. <br> | <table><tr><td colspan='2'>[[4lce]] is a 1 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=4LCE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LCE FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KMT:4-(METHYLSULFANYL)-2-OXOBUTANOIC+ACID'>KMT</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.38Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KMT:4-(METHYLSULFANYL)-2-OXOBUTANOIC+ACID'>KMT</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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=4lce FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lce OCA], [https://pdbe.org/4lce PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lce RCSB], [https://www.ebi.ac.uk/pdbsum/4lce PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lce ProSAT]</span></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=4lce FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lce OCA], [https://pdbe.org/4lce PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lce RCSB], [https://www.ebi.ac.uk/pdbsum/4lce PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lce ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/CTBP1_HUMAN CTBP1_HUMAN] Involved in controlling the equilibrium between tubular and stacked structures in the Golgi complex. Functions in brown adipose tissue (BAT) differentiation. Corepressor targeting diverse transcription regulators such as GLIS2. Has dehydrogenase activity.<ref>PMID:9858600</ref> <ref>PMID:15542832</ref> <ref>PMID:19103759</ref> <ref>PMID:12419229</ref> | [https://www.uniprot.org/uniprot/CTBP1_HUMAN CTBP1_HUMAN] Involved in controlling the equilibrium between tubular and stacked structures in the Golgi complex. Functions in brown adipose tissue (BAT) differentiation. Corepressor targeting diverse transcription regulators such as GLIS2. Has dehydrogenase activity.<ref>PMID:9858600</ref> <ref>PMID:15542832</ref> <ref>PMID:19103759</ref> <ref>PMID:12419229</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The oncogenic corepressors C-terminal Binding Protein (CtBP) 1 and 2 harbor regulatory d-isomer specific 2-hydroxyacid dehydrogenase (d2-HDH) domains. 4-Methylthio 2-oxobutyric acid (MTOB) exhibits substrate inhibition and can interfere with CtBP oncogenic activity in cell culture and mice. Crystal structures of human CtBP1 and CtBP2 in complex with MTOB and NAD+ revealed two key features: a conserved tryptophan that likely contributes to substrate specificity and a hydrophilic cavity that links MTOB with an NAD+ phosphate. Neither feature is present in other d2-HDH enzymes. These structures thus offer key opportunities for the development of highly selective anti-neoplastic CtBP inhibitors. | ||
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| - | Crystal structures of human CtBP in complex with substrate MTOB reveal active site features useful for inhibitor design.,Hilbert BJ, Grossman SR, Schiffer CA, Royer WE Jr FEBS Lett. 2014 Mar 19. pii: S0014-5793(14)00231-2. doi:, 10.1016/j.febslet.2014.03.026. PMID:24657618<ref>PMID:24657618</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4lce" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
CtBP1 in complex with substrate MTOB
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