5x73: Difference between revisions
From Proteopedia
Jump to navigationJump to search
m Protected "5x73" [edit=sysop:move=sysop] |
No edit summary |
||
| Line 1: | Line 1: | ||
The | ==The crystal Structure PDE delta in complex with R-p9== | ||
<StructureSection load='5x73' size='340' side='right' caption='[[5x73]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5x73]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X73 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5X73 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=P59:(2R)-2-(2-fluorophenyl)-3-phenyl-1,2-dihydroquinazolin-4-one'>P59</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5x72|5x72]], [[5x74|5x74]]</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=5x73 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x73 OCA], [http://pdbe.org/5x73 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x73 RCSB], [http://www.ebi.ac.uk/pdbsum/5x73 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x73 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/PDE6D_HUMAN PDE6D_HUMAN]] Acts as a GTP specific dissociation inhibitor (GDI). Increases the affinity of ARL3 for GTP by several orders of magnitude and does so by decreasing the nucleotide dissociation rate. Stabilizes Arl3-GTP by decreasing the nucleotide dissociation (By similarity). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Structural biology is a powerful tool for investigating the stereospecific interactions between a protein and its ligand. Herein, an unprecedented chiral binding pattern was observed for inhibitors of KRAS-PDEdelta interactions. Virtual screening and X-ray crystallography studies revealed that two enantiomers of a racemic inhibitor could bind at different sites. Fragment-based drug design was used to identify highly potent PDEdelta inhibitors that can be used as promising lead compounds for target validation and antitumor drug development. | |||
Structural Biology-Inspired Discovery of Novel KRAS-PDEdelta Inhibitors.,Jiang Y, Zhuang C, Chen L, Lu J, Dong G, Miao Z, Zhang W, Li J, Sheng C J Med Chem. 2017 Oct 3. doi: 10.1021/acs.jmedchem.7b01243. PMID:28929751<ref>PMID:28929751</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5x73" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Chen, L]] | |||
[[Category: Jiang, Y]] | |||
[[Category: Sheng, C]] | |||
[[Category: Wang, F]] | |||
[[Category: Wang, R]] | |||
[[Category: Zhuang, C]] | |||
[[Category: Lipid binding protein]] | |||
Revision as of 09:18, 4 October 2017
The crystal Structure PDE delta in complex with R-p9
| ||||||||||||
