Imatinib da structurally similar to ATP, competes with ATP for the occupation of its specific binding pocket within the kinase domain of the BCR-ABL protein.
Instead of ATP, imatinib (IM) occupies the binding pocket within the BCR-ABL and phosphorylation of tyrosine molecules cannot take place.
Please login to access all articles, images, and functions.
Our content is available exclusively to medical professionals. If you have already registered, please login. If you haven't, you can register for free (medical professionals only).
Please complete your registration to access all articles and images.
To gain access, you must complete your registration. You either haven't confirmed your e-mail address or we still need proof that you are a member of the medical profession.