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Literature summary for 2.7.11.13 extracted from

  • Leonard, T.A.; Rozycki, B.; Saidi, L.F.; Hummer, G.; Hurley, J.H.
    Crystal structure and allosteric activation of protein kinase C betaII (2011), Cell, 144, 55-66.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.11.13

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Sf9 cells as a GST-fusion protein Rattus norvegicus

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
DELTA621-622 deletion of two residues in the AGC linker that passes through the cleft of the C1B domain (DELTA621–622) results in a 2fold decrease in the concentration of phorbol 12-myristate 13-acetate required to mediate half-maximal translocation Rattus norvegicus
F629D within the NFD helix, mutant F629D and mutant F633D lead to 2- to 5fold decrease in EC50 for phorbol 12-myristate 13-acetate induced translocation Rattus norvegicus
F633D within the NFD helix, mutant F629D and mutant F633D lead to 2- to 5fold decrease in EC50 for phorbol 12-myristate 13-acetate induced translocation Rattus norvegicus
L125D mutation of Leu125 in the C1B domain, which is part of the C1B clamp interface, increases EC50 for phorbol 12-myristate 13-acetate induced translocation more than 10fold Rattus norvegicus
L358D mutation of residues in the hydrophobic interface between the kinase N lobe and the C1B domain (L358D, L367D, Y422D, Y430D) results in 5- to 14fold decrease in the EC50 for phorbol 12-myristate 13-acetate induced translocation Rattus norvegicus
L367D mutation of residues in the hydrophobic interface between the kinase N lobe and the C1B domain (L358D, L367D, Y422D, Y430D) results in 5- to 14fold decrease in the EC50 for phorbol 12-myristate 13-acetate induced translocation Rattus norvegicus
Y422D mutation of residues in the hydrophobic interface between the kinase N lobe and the C1B domain (L358D, L367D, Y422D, Y430D) results in 5- to 14fold decrease in the EC50 for phorbol 12-myristate 13-acetate induced translocation Rattus norvegicus
Y430D mutation of residues in the hydrophobic interface between the kinase N lobe and the C1B domain (L358D, L367D, Y422D, Y430D) results in 5- to 14fold decrease in the EC50 for phorbol 12-myristate 13-acetate induced translocation Rattus norvegicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
78000
-
 SDS-PAGE Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
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-
-

Purification (Commentary)

Purification (Comment) Organism
anion-exchange chromatography and gel filtration Rattus norvegicus

Subunits

Subunits Comment Organism
monomer
-
 Rattus norvegicus

Synonyms

Synonyms Comment Organism
PKC betaII
-
 Rattus norvegicus