Tyrosine Kinases are hot topic these days. Cancer, arthritis, lupus….What else will scientists figure out about this tyrosine phosphorylating protein.

EGFR Tyrosine Kinase

Here we see two Tyrosine Kinases, an inactive and active mutant form of the protein. Mutations of TK’s are common and increasingly due to drugs that bind too strongly to it and cause conformation changes that progressively prevent drugs from working.

Comparing the datasets, it’s clear how the AS-H1 Loop changes shape in ways to make its active Tyrosine residue (a common active site of these kinases) available for phosphorylation by ATP. The reason for such a drastic shape change in the protein is clearly associated with the drugs you see bound to each protein.  One drug seems to effectively inactivate the kinase, thereby suppressing cellular proliferation….aka cancer.

Photos of EGFR Tyrosine Kinase 3D Prints

The other remains active, showing a wide-open binding pocket and clear access to its tyrosine residue.  The Active Mutant version has a drug bound to it that separates two portions of the protein’s chain cause the AS-H1 Loop to lock into an Active state.

Bruton’s Tyrosine Kinase

Here we see a different Tyrosine Kinase, Bruton’s Tyrosine Kinase. This is a kinase found in different cells than EGFR, but exhibits the same tyrosine residue, structural homology, and AS-H1 loop. Here you can see how loosely the drug binds into the pocket, allowing for it to reversibly bind to Btk, a unique biochemical property for a TK inhibitor.

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