Sandbox 210: Difference between revisions

Cdk5 gene has been mapped to chromosome seven. The Cdk5 protein is a 33 kDa molecule with kinase activity when bound to its activators. Activated Cdk5 phosphorylates serine and threonine that have a proline immediately downstream. This proline is an obligatory requirement while the basic residues, lysine and arginine, are preferred at upstream position +3. Cdk5 phosphorylates serine and threonine in the motif S/TPXK/R where S and T are serine–threonine that can be phosphorylated (X is any amino acid and P is the obligatory proline present at position +1). Like most eukaryotic protein kinases, Cdk5 has a catalytic domain flanked with additional domains that are involved in its regulation. The catalytic domain has an N-terminal lobe of beta-sheet and alpha-helical C-domain (C lobe) with an ATP binding site between the two. The alpha-helical structure is called PSAALRE based on the polypeptide sequence. A stretch of 20 residues located centrally at the interphase of N and C lobe can acquire a conformation competent for phosphate transfer and is called the activation loop.<ref name="un" />