Title : Potent inhibition of human sulfotransferase 1A1 by 17α-ethinylestradiol: role of 3'-phosphoadenosine 5'-phosphosulfate binding and structural rearrangements in regulating inhibition and activity.

Pub. Date : 2012 Aug

PMID : 22593037






4 Functional Relationships(s)
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1 Potent inhibition of human sulfotransferase 1A1 by 17alpha-ethinylestradiol: role of 3"-phosphoadenosine 5"-phosphosulfate binding and structural rearrangements in regulating inhibition and activity. Phosphoadenosine Phosphosulfate sulfotransferase family 1A member 1 Homo sapiens
2 The K(d) for E2 binding to SULT1A1 changed from 2.3 +- 0.9 to 1.2 +- 0.56 muM in the presence of PAP. Phosphoadenosine Phosphosulfate sulfotransferase family 1A member 1 Homo sapiens
3 Docking studies with E2 indicate that E2 binds in a competent orientation in the resolved structure of SULT1A1 in the both presence and absence of 3"-phosphoadenosine 5"-phosphosulfate (PAPS). Phosphoadenosine Phosphosulfate sulfotransferase family 1A member 1 Homo sapiens
4 Docking studies with E2 indicate that E2 binds in a competent orientation in the resolved structure of SULT1A1 in the both presence and absence of 3"-phosphoadenosine 5"-phosphosulfate (PAPS). Phosphoadenosine Phosphosulfate sulfotransferase family 1A member 1 Homo sapiens