1. Pan2 exploits the asymmetry and forms an extensive interface with the Pan3 dimerStructural details of the complex of ctPan3 PKC bound to the Pan3 interacting domain (PID) of ctPan2. ctPan2 is shown in red, and ctPan3 PKC chains A and B are depicted in wheat and cyan, respectively.
Pan2 exploits the asymmetry and forms an extensive interface with the Pan3 dimerStructural details of the complex of ctPan3 PKC bound to the Pan3 interacting domain (PID) of ctPan2. ctPan2 is shown in red, and ctPan3 PKC chains A and B are depicted in wheat and cyan, respectively. Close‐up view of the four‐stranded intermolecular antiparallel β‐sheet formed between a β‐hairpin in ctPan2 (residues 384–393) and a β‐hairpin ear in ctPan3 chain B (residues 597–612). Overall structure of the ctPan3 PKC dimer bound to ctPan2 PID (cartoon). ATP is in ball and stick representation. The N‐terminal region of ctPan2 PID interacts with the ctPan3 dimer by inserting aromatic residues Phe357 and Trp360 (stick representation) into two pockets formed between the coiled coil and the CTD of ctPan3 chain A. Surface representation of the CTD of ctPan3 chain B colored by sequence conservation. ctPan2 PID (residues 400–402) binds into a conserved groove in the CTD. Superposition of ctPan3 from the structures of isolated ctPan3 (black) and bound to ctPan2 PID (Pan3 in cyan and wheat, Pan2 in red) in cartoon representation. The N‐terminus of chain B of the ctPan3 dimer rotates by approximately 90° upon binding of ctPan2 to form an antiparallel β‐sheet with ctPan2.
Jana Wolf et al. EMBO J. 2014;33:
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