9h48
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Mouse Iodothyronine deiodinase 2 catalytic core, mutant - LysLys180AlaAla, Secys-> Cys== | |
| + | <StructureSection load='9h48' size='340' side='right'caption='[[9h48]], [[Resolution|resolution]] 1.09Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9h48]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9H48 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9H48 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]] 1.09Å</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=9h48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9h48 OCA], [https://pdbe.org/9h48 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9h48 RCSB], [https://www.ebi.ac.uk/pdbsum/9h48 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9h48 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/IOD2_MOUSE IOD2_MOUSE] Responsible for the deiodination of T4 (3,5,3',5'-tetraiodothyronine) into T3 (3,5,3'-triiodothyronine). Essential for providing the brain with appropriate levels of T3 during the critical period of development. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Iodothyronine deiodinases (Dio) are selenocysteine-containing membrane enzymes that activate and inactivate the thyroid hormones (TH) through reductive iodide eliminations. The three deiodinase isoforms are homodimers sharing highly conserved amino acid sequences, but they differ in their regioselectivities for the deiodination reaction and regulatory features. We have now solved a crystal structure of the mouse deiodinase 2 (Dio2) catalytic domain. It reveals a high overall similarity to the deiodinase 3 structure, supporting the proposed common mechanism, but also Dio2-specific features, likely mediating its unique properties. Activity studies with an artificially enforced Dio dimer further confirm that dimerization is required for activity and requires both the catalytic core and the enzyme's N-terminus. Cross-linking studies reveal the catalytic core's dimerization interface, providing insights into the architecture of the complete, active Dio homodimer. | ||
| - | + | Structural Insights into the Iodothyronine Deiodinase 2 Catalytic Core and Deiodinase Catalysis and Dimerization.,Towell H, Braun D, Brol A, di Fonzo A, Rijntjes E, Kohrle J, Schweizer U, Steegborn C Biomolecules. 2024 Oct 28;14(11):1373. doi: 10.3390/biom14111373. PMID:39595550<ref>PMID:39595550</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 9h48" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Steegborn C]] | ||
| + | [[Category: Towell H]] | ||
Current revision
Mouse Iodothyronine deiodinase 2 catalytic core, mutant - LysLys180AlaAla, Secys-> Cys
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