Title : Comparative study of the binding mode between cytochrome P450 17A1 and prostate cancer drugs in the absence of haem iron.

Pub. Date : 2019 Oct

PMID : 30431391






4 Functional Relationships(s)
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1 According to the X-ray crystal structures of CYP17A1 (including its complexes with inhibitors), it is shown that a hydrogen bond exists between CYP17A1 and its inhibitors (such as abiraterone and TOK-001). Hydrogen cytochrome P450 family 17 subfamily A member 1 Homo sapiens
2 According to the X-ray crystal structures of CYP17A1 (including its complexes with inhibitors), it is shown that a hydrogen bond exists between CYP17A1 and its inhibitors (such as abiraterone and TOK-001). Hydrogen cytochrome P450 family 17 subfamily A member 1 Homo sapiens
3 In the case of abiraterone binding, the unfilled volume in the active site cavity increases the freedom of movement of abiraterone within CYP17A1, leading to the collective motions of the helices G and B" as well as the breaking of hydrogen bond existing between the 3beta-OH group of abiraterone and N202 of CYP17A1. Hydrogen cytochrome P450 family 17 subfamily A member 1 Homo sapiens
4 In the case of abiraterone binding, the unfilled volume in the active site cavity increases the freedom of movement of abiraterone within CYP17A1, leading to the collective motions of the helices G and B" as well as the breaking of hydrogen bond existing between the 3beta-OH group of abiraterone and N202 of CYP17A1. Hydrogen cytochrome P450 family 17 subfamily A member 1 Homo sapiens