Purpose:

The non-receptor protein tyrosine phosphatase (SHP2) was the first reported oncogenic tyrosine phosphatase and is very important in signal transduction. Shp2 contains two N-terminally located Src-homology 2 domains (N-SH2 and C-SH2), and a central phosphor-tyrosine phosphatase (PTP) domain. The N-SH2 domain blocks access to the catalytic site (Cys 459) by covering the PTP domain so that SHP2 will stay inactive. SHP099 is a molecule which can stabilize SHP2 in an auto-inhibited conformation. SHP099 concurrently binds to the interface of the N-SH2, C-SH2, and PTP domains, thus inhibiting SHP2 activity through an allosteric mechanism.

Medium:

VMD, Keyshot, Adobe Photoshop

Audience:

Biology Major Undergraduate