4jrg: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[4jrg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JRG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JRG FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=I09:(3R,4R,5S)-3-(3-CHLOROPHENYL)-4-(4-CHLOROPHENYL)-4-CYANO-N-[(3S)-3,4-DIHYDROXYBUTYL]-5-(2,2-DIMETHYLPROPYL)-D-PROLINAMIDE'>I09</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]] 1.9&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=I09:(3R,4R,5S)-3-(3-CHLOROPHENYL)-4-(4-CHLOROPHENYL)-4-CYANO-N-[(3S)-3,4-DIHYDROXYBUTYL]-5-(2,2-DIMETHYLPROPYL)-D-PROLINAMIDE'>I09</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=4jrg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jrg OCA], [https://pdbe.org/4jrg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jrg RCSB], [https://www.ebi.ac.uk/pdbsum/4jrg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jrg ProSAT]</span></td></tr>
 </table>
 == Function ==
 [https://www.uniprot.org/uniprot/MDM2_XENLA MDM2_XENLA] E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degration by the proteasome (By similarity).
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Restoration of p53 activity by inhibition of the p53-MDM2 interaction has been considered an attractive approach for cancer treatment. However, the hydrophobic protein-protein interaction surface represents a significant challenge for the development of small-molecule inhibitors with desirable pharmacological profiles. RG7112 was the first small-molecule p53-MDM2 inhibitor in clinical development. Here, we report the discovery and characterization of a second generation clinical MDM2 inhibitor, RG7388, with superior potency and selectivity.
-Discovery of RG7388, a Potent and Selective p53-MDM2 Inhibitor in Clinical Development.,Ding Q, Zhang Z, Liu JJ, Jiang N, Zhang J, Ross TM, Chu XJ, Bartkovitz D, Podlaski F, Janson C, Tovar C, Filipovic ZM, Higgins B, Glenn K, Packman K, Vassilev LT, Graves B J Med Chem. 2013 Jul 16. PMID:23808545<ref>PMID:23808545</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4jrg" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[MDM2 3D structures|MDM2 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>