Literature summary for 2.3.2.27 extracted from

Temboot, P.; Lee, R.F.S.; Menin, L.; Patiny, L.; Dyson, P.J.; Ratanaphan, A.
Biochemical and biophysical characterization of ruthenation of BRCA1 RING protein by RAPTA complexes and its E3 ubiquitin ligase activity (2017), Biochem. Biophys. Res. Commun., 488, 355-361 .

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Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	binding of the RAPTA compounds, i.e. Ru(h6-arene)(1,3,5-triaza-7-phosphaadamantane)Cl2, to the BRCA1 protein results in a release of Zn2+ ions in a dose- and time-dependent manner, as well as thermal alteration of ruthenated-BRCA1 proteins. The preferential binding sites of the RAPTA complexes on the BRCA1 zinc finger RING domain are at a short peptide stretch, Cys24-Lys25-Phe26-Cys27-Met28-Leu29 and Lys35 (residues 44-49 and 55 on full length BRCA1). Binding results in inactivation of the RING heterodimer BRCA1/BARD1-mediated E3 ubiquitin ligase function	Homo sapiens
RAPTA-C	-	Homo sapiens
RAPTA-EA1	the IC50 value for inactivation of E3 ubiquitin ligase activity by RAPTA-EA1 is markedly lower than the corresponding values for RAPTA-C, RAPTA-T and cisplatin	Homo sapiens
RAPTA-T	-	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P38398	isoform BRCA1	-

Synonyms

Synonyms	Comment	Organism
BRCA1	-	Homo sapiens
breast cancer type 1 susceptibility protein	-	Homo sapiens

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Release 2023.1 (January 2023)