Structural highlights
Function
[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).
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jiang Y, Zhuang C, Chen L, Lu J, Dong G, Miao Z, Zhang W, Li J, Sheng C. Structural Biology-Inspired Discovery of Novel KRAS-PDEdelta Inhibitors. J Med Chem. 2017 Oct 3. doi: 10.1021/acs.jmedchem.7b01243. PMID:28929751 doi:http://dx.doi.org/10.1021/acs.jmedchem.7b01243
