7nto

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:01, 17 October 2024) (edit) (undo)
 
(One intermediate revision not shown.)
Line 3: Line 3:
<StructureSection load='7nto' size='340' side='right'caption='[[7nto]], [[Resolution|resolution]] 1.23&Aring;' scene=''>
<StructureSection load='7nto' size='340' side='right'caption='[[7nto]], [[Resolution|resolution]] 1.23&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[7nto]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NTO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NTO FirstGlance]. <br>
+
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NTO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NTO FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.23&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <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=7nto FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nto OCA], [https://pdbe.org/7nto PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nto RCSB], [https://www.ebi.ac.uk/pdbsum/7nto PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nto 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=7nto FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nto OCA], [https://pdbe.org/7nto PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nto RCSB], [https://www.ebi.ac.uk/pdbsum/7nto PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nto ProSAT]</span></td></tr>
</table>
</table>
-
== Function ==
 
-
[[https://www.uniprot.org/uniprot/TRM2A_HUMAN TRM2A_HUMAN]] May be involved in nucleic acid metabolism and/or modifications.
 
-
<div style="background-color:#fffaf0;">
 
-
== Publication Abstract from PubMed ==
 
-
Polyglutamine (polyQ) diseases are characterized by an expansion of cytosine-adenine-guanine (CAG) trinucleotide repeats encoding for an uninterrupted prolonged polyQ tract. We previously identified TRMT2A as a strong modifier of polyQ-induced toxicity in an unbiased large-scale screen in Drosophila melanogaster. This work aimed at identifying and validating pharmacological TRMT2A inhibitors as treatment opportunities for polyQ diseases in humans. Computer-aided drug discovery was implemented to identify human TRMT2A inhibitors. Additionally, the crystal structure of one protein domain, the RNA recognition motif (RRM), was determined, and Biacore experiments with the RRM were performed. The identified molecules were validated for their potency to reduce polyQ aggregation and polyQ-induced cell death in human HEK293T cells and patient derived fibroblasts. Our work provides a first step towards pharmacological inhibition of this enzyme and indicates TRMT2A as a viable drug target for polyQ diseases.
 
- 
-
Small-molecule modulators of TRMT2A decrease PolyQ aggregation and PolyQ-induced cell death.,Margreiter MA, Witzenberger M, Wasser Y, Davydova E, Janowski R, Metz J, Habib P, Sahnoun SEM, Sobisch C, Poma B, Palomino-Hernandez O, Wagner M, Carell T, Jon Shah N, Schulz JB, Niessing D, Voigt A, Rossetti G Comput Struct Biotechnol J. 2021 Dec 28;20:443-458. doi:, 10.1016/j.csbj.2021.12.029. eCollection 2022. PMID:35070167<ref>PMID:35070167</ref>
 
- 
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
-
</div>
 
-
<div class="pdbe-citations 7nto" style="background-color:#fffaf0;"></div>
 
-
== References ==
 
-
<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Davydova, E]]
+
[[Category: Davydova E]]
-
[[Category: Janowski, R]]
+
[[Category: Janowski R]]
-
[[Category: Niessing, D]]
+
[[Category: Niessing D]]
-
[[Category: Witzenberger, M]]
+
[[Category: Witzenberger M]]
-
[[Category: Methyltransferase]]
+
-
[[Category: Polyq aggregation]]
+
-
[[Category: Transferase]]
+
-
[[Category: Trmt2a]]
+
-
[[Category: Trna binding]]
+

Current revision

The structure of RRM domain of human TRMT2A at 1.23 A resolution

PDB ID 7nto

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools