Article
Insights into the key interactions between human protein phosphatase 5 and cantharidin using molecular dynamics and site-directed mutagenesis bioassays.
Scientific reports - 20 Jul 2015
Liu Ji-Yuan, Chen Xi-En, Zhang Ya-Lin
Abstract excerpt
Serine/threonine protein phosphatase 5 (PP5) is a promising novel target for anticancer therapies. This work aims to uncover the key interactions at the atomic level between PP5 and three inhibitors (cantharidin, norcantharidin and endothall). We found that, unlike previous report, Arg 100 contributes less to PP5-inhibitor binding, and the residues His 69, Asn 128, His 129, Arg 225, His 252 and Arg 250 are of...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
