Pub. Date : 2019 Oct
PMID : 30431391
18 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 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). | abiraterone | 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). | abiraterone | cytochrome P450 family 17 subfamily A member 1 | Homo sapiens |
| 3 | Previous short MD simulations (50 ns) suggested that the binding of abiraterone to CYP17A1 is stronger than that of TOK-001. | abiraterone | cytochrome P450 family 17 subfamily A member 1 | Homo sapiens |
| 4 | In this work, by carrying out long atomistic MD simulations (200 ns) of CYP17A1 and its complexes with abiraterone and TOK-001, we observed a binding mode between CYP17A1 and abiraterone, which is different from the binding mode between CYP17A1 and TOK-001. | abiraterone | cytochrome P450 family 17 subfamily A member 1 | Homo sapiens |
| 5 | In this work, by carrying out long atomistic MD simulations (200 ns) of CYP17A1 and its complexes with abiraterone and TOK-001, we observed a binding mode between CYP17A1 and abiraterone, which is different from the binding mode between CYP17A1 and TOK-001. | abiraterone | cytochrome P450 family 17 subfamily A member 1 | Homo sapiens |
| 6 | In this work, by carrying out long atomistic MD simulations (200 ns) of CYP17A1 and its complexes with abiraterone and TOK-001, we observed a binding mode between CYP17A1 and abiraterone, which is different from the binding mode between CYP17A1 and TOK-001. | abiraterone | cytochrome P450 family 17 subfamily A member 1 | Homo sapiens |
| 7 | In this work, by carrying out long atomistic MD simulations (200 ns) of CYP17A1 and its complexes with abiraterone and TOK-001, we observed a binding mode between CYP17A1 and abiraterone, which is different from the binding mode between CYP17A1 and TOK-001. | abiraterone | cytochrome P450 family 17 subfamily A member 1 | Homo sapiens |
| 8 | In this work, by carrying out long atomistic MD simulations (200 ns) of CYP17A1 and its complexes with abiraterone and TOK-001, we observed a binding mode between CYP17A1 and abiraterone, which is different from the binding mode between CYP17A1 and TOK-001. | abiraterone | cytochrome P450 family 17 subfamily A member 1 | Homo sapiens |
| 9 | In this work, by carrying out long atomistic MD simulations (200 ns) of CYP17A1 and its complexes with abiraterone and TOK-001, we observed a binding mode between CYP17A1 and abiraterone, which is different from the binding mode between CYP17A1 and TOK-001. | abiraterone | cytochrome P450 family 17 subfamily A member 1 | Homo sapiens |
| 10 | 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. | abiraterone | cytochrome P450 family 17 subfamily A member 1 | Homo sapiens |
| 11 | 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. | abiraterone | cytochrome P450 family 17 subfamily A member 1 | Homo sapiens |
| 12 | 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. | abiraterone | cytochrome P450 family 17 subfamily A member 1 | Homo sapiens |
| 13 | 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. | abiraterone | cytochrome P450 family 17 subfamily A member 1 | Homo sapiens |
| 14 | 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. | abiraterone | cytochrome P450 family 17 subfamily A member 1 | Homo sapiens |
| 15 | 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. | abiraterone | cytochrome P450 family 17 subfamily A member 1 | Homo sapiens |
| 16 | By pulling the two inhibitors (abiraterone and TOK-001) out of the binding pocket in CYP17A1, we discovered that abiraterone and TOK-001 were moved from their binding sites to the surface of protein similarly through the channels formed by the helices G and B". | abiraterone | cytochrome P450 family 17 subfamily A member 1 | Homo sapiens |
| 17 | By pulling the two inhibitors (abiraterone and TOK-001) out of the binding pocket in CYP17A1, we discovered that abiraterone and TOK-001 were moved from their binding sites to the surface of protein similarly through the channels formed by the helices G and B". | abiraterone | cytochrome P450 family 17 subfamily A member 1 | Homo sapiens |
| 18 | In addition, based on the free energy calculations, one can see that it is energetically favorable for the two inhibitors (abiraterone and TOK-001) to enter into the binding pocket in CYP17A1. | abiraterone | cytochrome P450 family 17 subfamily A member 1 | Homo sapiens |