Extended Data Fig. 3: N-terminal helix 1 extends a positively charged patch on PTEN.
From: The structural basis of PTEN regulation by multi-site phosphorylation
a, b, c, d, structures of ncrPTEN-13sp-T1, 4p-crPTEN-13sp-T2, 4p-crPTEN-20sp-T3, 4p-crPTEN-22sp-T3 in ribbons with the width of the tube proportional to b-factors. The N-terminal helix, loop of catalytic domain, and CBRIII display the highest spread. e, surface representation of PTEN 1D5R colored as the electrostatic potential with the N-terminal helix area of 4p-crPTEN-13sp-T2 (PDB ID 7JUK) marked as a yellow box. The tartrate molecule observed in 1D5R bound to active site is shown as orange sticks. f, surface representation of 4p-crPTEN-13sp-T2 colored as the electrostatic potential displays how the N-terminal helix closes up the tartrate binding site observed in 1D5R. Tartrate is not a component of the crystallization mix of 7JUL.
