8fur
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of human IDO1 with compound 11== | |
| + | <StructureSection load='8fur' size='340' side='right'caption='[[8fur]], [[Resolution|resolution]] 2.29Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8fur]] is a 4 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=8FUR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8FUR FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=Y9X:N-(4-methylphenyl)-N-[(1P,2P)-4-propoxy-5-propyl-2-(1H-tetrazol-5-yl)[1,1-biphenyl]-3-yl]urea'>Y9X</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=8fur FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8fur OCA], [https://pdbe.org/8fur PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8fur RCSB], [https://www.ebi.ac.uk/pdbsum/8fur PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8fur ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/I23O1_HUMAN I23O1_HUMAN] Catalyzes the cleavage of the pyrrol ring of tryptophan and incorporates both atoms of a molecule of oxygen.<ref>PMID:17671174</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Starting from the dialkylaniline indoleamine 2,3-dioxygenase 1 (IDO1) inhibitor lead 3 (IDO1 HeLa IC(50) = 7.0 nM), an iterative process of synthesis and screening led to cyclized analog 21 (IDO1 HeLa IC(50) = 3.6 nM) which maintained the high potency of 3 while addressing issues of lipophilicity, cytochrome P450 (CYP) inhibition, hERG (human potassium ion channel Kv11.1) inhibition, Pregnane X Receptor (PXR) transactivation, and oxidative metabolic stability. An x-ray crystal structure of a biaryl alkyl ether 11 bound to IDO1 was obtained. Consistent with our earlier results, compound 11 was shown to bind to the apo form of the enzyme. | ||
| - | + | Synthesis and biological evaluation of biaryl alkyl ethers as inhibitors of IDO1.,Markwalder JA, Balog AJ, Williams DK, Nara SJ, Reddy R, Roy S, Kanyaboina Y, Li X, Johnston K, Fan Y, Lewis H, Marsilio F, Yan C, Critton D, Newitt JA, Traeger SC, Wu DR, Jure-Kunkel MN, Jayaraman L, Lin TA, Sinz MW, Hunt JT, Seitz SP Bioorg Med Chem Lett. 2023 Apr 11;88:129280. doi: 10.1016/j.bmcl.2023.129280. PMID:37054759<ref>PMID:37054759</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8fur" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Critton DA]] | ||
| + | [[Category: Lewis HA]] | ||
Current revision
Crystal structure of human IDO1 with compound 11
| |||||||||||
