Structural highlights
Publication Abstract from PubMed
The probe-based discovery of the first small-molecule inhibitor of the repair enzyme 8-oxo-dGTPase (MTH1) is presented, which is an unconventional cyclometalated ruthenium half-sandwich complex. The organometallic inhibitor with low-nanomolar activity displays astonishing specificity, as verified in tests with an extended panel of protein kinases and other ATP binding proteins. The binding of the organometallic inhibitor to MTH1 is investigated by protein crystallography.
An organometallic inhibitor for the human repair enzyme 7,8-dihydro-8-oxoguanosine triphosphatase.,Streib M, Kraling K, Richter K, Xie X, Steuber H, Meggers E Angew Chem Int Ed Engl. 2014 Jan 3;53(1):305-9. doi: 10.1002/anie.201307849. Epub, 2013 Nov 20. PMID:24258965[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Streib M, Kraling K, Richter K, Xie X, Steuber H, Meggers E. An organometallic inhibitor for the human repair enzyme 7,8-dihydro-8-oxoguanosine triphosphatase. Angew Chem Int Ed Engl. 2014 Jan 3;53(1):305-9. doi: 10.1002/anie.201307849. Epub, 2013 Nov 20. PMID:24258965 doi:http://dx.doi.org/10.1002/anie.201307849
