Pub. Date : 2004 Jun 2
PMID : 15141161
5 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Binding of the peptide also induces a hinge motion between the N- and C-terminal domains of JNK1 and distorts the ATP-binding cleft, reducing the affinity of the kinase for ATP. | Adenosine Triphosphate | mitogen-activated protein kinase 8 | Homo sapiens |
| 2 | Binding of the peptide also induces a hinge motion between the N- and C-terminal domains of JNK1 and distorts the ATP-binding cleft, reducing the affinity of the kinase for ATP. | Adenosine Triphosphate | mitogen-activated protein kinase 8 | Homo sapiens |
| 3 | In addition, we also determined the ternary complex structure of pepJIP1-bound JNK1 complexed with SP600125, an ATP-competitive inhibitor of JNK, providing the basis for the JNK specificity of the compound. | Adenosine Triphosphate | mitogen-activated protein kinase 8 | Homo sapiens |
| 4 | In addition, we also determined the ternary complex structure of pepJIP1-bound JNK1 complexed with SP600125, an ATP-competitive inhibitor of JNK, providing the basis for the JNK specificity of the compound. | Adenosine Triphosphate | mitogen-activated protein kinase 8 | Homo sapiens |
| 5 | In addition, we also determined the ternary complex structure of pepJIP1-bound JNK1 complexed with SP600125, an ATP-competitive inhibitor of JNK, providing the basis for the JNK specificity of the compound. | Adenosine Triphosphate | mitogen-activated protein kinase 8 | Homo sapiens |