This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1uk1
From Proteopedia
|
Crystal structure of human poly(ADP-ribose) polymerase complexed with a potent inhibitor
Contents |
Overview
A novel class of quinazolinone derivatives as potent, poly(ADP-ribose)polymerase-1 (PARP-1) inhibitors has been discovered. Key, to success was application of a rational discovery strategy involving, structure-based design, combinatorial chemistry, and classical SAR for, improvement of potency and bioavailability. The new inhibitors were shown, to bind to the nicotinamide-ribose binding site (NI site) and the, adenosine-ribose binding site (AD site) of NAD+.
Disease
Known diseases associated with this structure: Xeroderma pigmentosum (1) OMIM:[173870]
About this Structure
1UK1 is a Single protein structure of sequence from Homo sapiens with as ligand. Active as NAD(+) ADP-ribosyltransferase, with EC number 2.4.2.30 Full crystallographic information is available from OCA.
Reference
Rational approaches to discovery of orally active and brain-penetrable quinazolinone inhibitors of poly(ADP-ribose)polymerase., Hattori K, Kido Y, Yamamoto H, Ishida J, Kamijo K, Murano K, Ohkubo M, Kinoshita T, Iwashita A, Mihara K, Yamazaki S, Matsuoka N, Teramura Y, Miyake H, J Med Chem. 2004 Aug 12;47(17):4151-4. PMID:15293985
Page seeded by OCA on Fri Feb 15 17:02:49 2008
