EC Number   |
|---|
   2.7.11.13 | - |
| 2.7.11.13 | crystal structure of full-length protein kinase C bII is determined at 4.0 A. The C1B domain clamps the NFD helix in a low activity conformation, which is reversed upon membrane binding. A low-resolution solution structure of the closed conformation of PKCbII is derived from small-angle X-ray scattering |
| 2.7.11.13 | crystal structure of PKC-delta C2 domain. Structural elements unique to this C2 domain include a helix and a protruding beta hairpin which may contribute basic sequences to a membrane-interaction site |
| 2.7.11.13 | crystal structure of PKCioata is determined at 2.4 A. The structure of the PKCiota/Par-3 peptide complex reveals that the kinase domain adopts an active conformation even though Thr402 in the activation loop is not phosphorylated. The Par-3 peptide binds to the groove between the N- and C-lobes of the kinase via combined hydrophobic and charge-charge interactions |
| 2.7.11.13 | crystal structure of PKCthetaC1B is determined to 1.63 A resolution. It is shown that, Trp253 at the rim of the activator-binding pocket is orientated towards the membrane |
| 2.7.11.13 | crystal structure of the cys2 activator-binding domain of protein kinase C delta in complex with phorbol ester |
| 2.7.11.13 | purified recombinant isozyme PKCbetaII catalytic domain, residues 321-673, hanging drop vapour diffusion method, 8 mg/ml protein in 0.1 M acetamidoiminodiacetic acid, pH 6.5, and 1.7-2.3 M sodium acetate, 19°C, X-ray diffraction structure determination and analysis at 3.2 A resolution, molecular replacement, modeling |
