5cte
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | ''' | + | ==Humanized yeast ACC carboxyltransferase domain bound to 2,2-dimethylpropyl (1S)-1-methyl-8-[(7-methyl-1H-indazol-5-yl)carbonyl]-2,8-diazaspiro[4.5]decane-2-carboxylate== |
| + | <StructureSection load='5cte' size='340' side='right' caption='[[5cte]], [[Resolution|resolution]] 2.34Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5cte]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CTE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CTE FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=57L:2,2-DIMETHYLPROPYL+(1S)-1-METHYL-8-[(7-METHYL-1H-INDAZOL-5-YL)CARBONYL]-2,8-DIAZASPIRO[4.5]DECANE-2-CARBOXYLATE'>57L</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ctb|5ctb]], [[5ctc|5ctc]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5cte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cte OCA], [http://pdbe.org/5cte PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cte RCSB], [http://www.ebi.ac.uk/pdbsum/5cte PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/ACAC_YEAST ACAC_YEAST]] Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase. Involved in the synthesis of very-long-chain fatty acid synthesis which is required to maintain a functional nuclear envelope. Required for acylation and vacuolar membrane association of VAC8 which is necessary to maintain a normal morphology of the vacuole.<ref>PMID:6108218</ref> <ref>PMID:6103540</ref> <ref>PMID:8943372</ref> <ref>PMID:10757783</ref> <ref>PMID:12730220</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | A novel series of spirocyclic-diamine based, isoform non-selective inhibitors of acetyl-CoA carboxylase (ACC) is described. These spirodiamine derivatives were discovered by design of a library to mimic the structural rigidity and hydrogen-bonding pattern observed in the co-crystal structure of spirochromanone inhibitor I. The lead compound 3.5.1 inhibited de novo lipogenesis in rat hepatocytes, with an IC50 of 0.30muM. | ||
| - | + | Discovery of spirocyclic-diamine inhibitors of mammalian acetyl CoA-carboxylase.,Kung DW, Griffith DA, Esler WP, Vajdos FF, Mathiowetz AM, Doran SD, Amor PA, Bagley SW, Banks T, Cabral S, Ford K, Garcia-Irizarry CN, Landis MS, Loomis K, McPherson K, Niosi M, Rockwell KL, Rose C, Smith AC, Southers JA, Tapley S, Tu M, Valentine JJ Bioorg Med Chem Lett. 2015 Sep 15. pii: S0960-894X(15)30067-6. doi:, 10.1016/j.bmcl.2015.09.035. PMID:26411795<ref>PMID:26411795</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5cte" style="background-color:#fffaf0;"></div> | |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Vajdos, F F]] | ||
| + | [[Category: Acc]] | ||
| + | [[Category: Inhibitor]] | ||
| + | [[Category: Transferase-transferase inhibitor complex]] | ||
Revision as of 03:53, 16 October 2015
Humanized yeast ACC carboxyltransferase domain bound to 2,2-dimethylpropyl (1S)-1-methyl-8-[(7-methyl-1H-indazol-5-yl)carbonyl]-2,8-diazaspiro[4.5]decane-2-carboxylate
| |||||||||||
