Role of the Pyrrolidine Ring of Proline in Determining the Substrate Specificity of cdc2 Kinase or cdk5

• Published in: Journal of biochemistry (Tokyo) Vol. 122; no. 2; pp. 409 - 414
• Main Authors: Ando, Shoji, Ikuhara, Toshihiko, Kamata, Tomoko, Sasaki, Yasuharu, Hisanaga, Shin-ichi, Kishimoto, Takeo, Ito, Hikaru, Inagaki, Masaki
• Format: Journal Article
• Language: English
• Published: England Oxford University Press 01.08.1997
• Subjects: cdc2 kinase; CDC2 Protein Kinase - chemistry; CDC2 Protein Kinase - metabolism; cdk 5; Computer Simulation; Cyclin-Dependent Kinase 5; Cyclin-Dependent Kinases; Kinetics; molecular dynamics and molecular mechanics simulations; Oligopeptides - chemical synthesis; Oligopeptides - metabolism; peptide synthesis; Phosphorylation; Proline - chemistry; Protein Structure, Secondary; Protein-Serine-Threonine Kinases - chemistry; Protein-Serine-Threonine Kinases - metabolism; Pyrrolidines - chemistry; Serine - metabolism; Substrate Specificity; Vimentin - metabolism

To examine structural features of proline which are essential for the proline-directed phosphorylation by cdc2 kinase or cdk5, we prepared the peptide representing the cdc2 kinase phosphorylation site at Ser-55 in vimentin [Ser-Leu-Tyr-Ser-Ser-Ser55-Pro56-Gly-Gly58-Ala-Tyr-NH2], the peptide containi...