9b96
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the human PAD2 protein bound to inhibitor== | |
| + | <StructureSection load='9b96' size='340' side='right'caption='[[9b96]], [[Resolution|resolution]] 1.64Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9b96]] 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=9B96 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9B96 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]] 1.64Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1AJA:(2~{R})-1-[[3-[(1~{S})-1-(2-bromophenyl)-3-[[2-methyl-5-(methylsulfonylamino)phenyl]amino]-3-oxidanylidene-propyl]-2-[3-(4-chloranylphenoxy)phenyl]benzimidazol-5-yl]methyl]-~{N}-methyl-pyrrolidine-2-carboxamide'>A1AJA</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=9b96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9b96 OCA], [https://pdbe.org/9b96 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9b96 RCSB], [https://www.ebi.ac.uk/pdbsum/9b96 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9b96 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PADI2_HUMAN PADI2_HUMAN] Catalyzes the deimination of arginine residues of proteins. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Peptidyl arginine deiminases (PADs) are important enzymes in many diseases, especially those involving inflammation and autoimmunity. Despite many years of effort, developing isoform-specific inhibitors has been a challenge. We describe herein the discovery of a potent, noncovalent PAD2 inhibitor, with selectivity over PAD3 and PAD4, from a DNA-encoded library. The biochemical and biophysical characterization of this inhibitor and two noninhibitory binders indicated a novel, Ca(2+) competitive mechanism of inhibition. This was confirmed via X-ray crystallographic analysis. Finally, we demonstrate that this inhibitor selectively inhibits PAD2 in a cellular context. | ||
| - | + | Discovery, Characterization, and Structure of a Cell Active PAD2 Inhibitor Acting through a Novel Allosteric Mechanism.,Byrnes LJ, Choi WY, Balbo P, Banker ME, Chang J, Chen S, Cheng X, Cong Y, Culp J, Di H, Griffor M, Hall J, Meng X, Morgan B, Mousseau JJ, Nicki J, O'Connell T, Ramsey S, Shaginian A, Shanker S, Trujillo J, Wan J, Vincent F, Wright SW, Vajdos F ACS Chem Biol. 2024 Sep 24. doi: 10.1021/acschembio.4c00397. PMID:39316753<ref>PMID:39316753</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 9b96" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Byrnes LJ]] | ||
| + | [[Category: Vajdos F]] | ||
Current revision
Crystal structure of the human PAD2 protein bound to inhibitor
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