Sentence examples for binds to the ATP-binding from inspiring English sources
One inhibitor, balanol, binds to the ATP-binding pocket.
This structural model indicates that the inhibitor strongly binds to the ATP-binding pocket of CDK9 and the structural comparison of the complex CDK2 flavopiridol correlates the structural differences with differences in inhibition of these CDKs by flavopiridol.
The structural model indicates that roscovitine strongly binds to the ATP-binding pocket of CDK5 and structural comparison of the CDK2 roscovitine complex correlates the structural differences with differences in inhibition of these CDKs by this inhibitor.
It has been shown that geldanamycin directly binds to the ATP-binding pocket in the N-terminal domain of Hsp90 [10] [10] and blocks the binding of nucleotides to Hsp90.
Like imatinib, sunitinib binds to the ATP-binding pocket of the KIT and PDGFRA kinases.
We previously reported that FK228 binds to the ATP-binding pocket of p110α based on a study with a docking model.
Chemical shift perturbation and NOE experiments demonstrated that the inhibitor binds to the ATP binding pocket.
In all structures, the compound binds to the ATP binding pocket of the FAK kinase and electron density for the compounds is well defined (see Fig. 2 for difference electron density of TAE226).
DOI: http://dx.doi.org/10.7554/eLife.05434.007 To further rule out off-target effects through which IPA might induce ER stress indirectly, we use a recently discovered IRE1α inhibitor, AD60, that binds to the ATP binding pocket of IRE1α's kinase domain, locking it into its inactive DFG/αC-out conformation and inhibiting its RNase activity (Dar et al., 2008; Korennykh et al., 2012).
A mutation, F1174C, suited in the C-terminal helix αC of ALK and distal from the small-molecule inhibitor ceritinib bound to the ATP-binding site, causes the emergence of drug resistance to ceritinib.
These structural models indicate that both inhibitors strongly bind to the ATP-binding pocket of CDK1 and structural comparison of the CDK complexes correlates the structures with differences in inhibition of these CDKs by flavopiridol and roscovitine.
