User:Michael Adams/Sandbox 1: Difference between revisions
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The structure of arginine kinase is mainly α-helical and contains an N-terminal region with a specificity loop for specific substrate binding. (Figure 1b). However, when compared to creatine kinase, arginine kinase is not terminated at the N-terminal end with a pair of proline-glycine residues. Typically within creatine kinase, the proline molecules restrict changes in conformation and is the amino acid that terminates helices. The glycine chains are usually associated with flexibility. However, in arginine kinase this is typically not the case. On the C-terminal end, there is an eight-stranded antiparallel β-sheet with seven α-helices flanking the sheet (Figure 1). | The structure of arginine kinase is mainly α-helical and contains an N-terminal region with a specificity loop for specific substrate binding. (Figure 1b). However, when compared to creatine kinase, arginine kinase is not terminated at the N-terminal end with a pair of proline-glycine residues. Typically within creatine kinase, the proline molecules restrict changes in conformation and is the amino acid that terminates helices. The glycine chains are usually associated with flexibility. However, in arginine kinase this is typically not the case. On the C-terminal end, there is an eight-stranded antiparallel β-sheet with seven α-helices flanking the sheet (Figure 1). | ||
[[Image:F1.large.jpg]][[Image:3M10 bio r 500.jpg]] | [[Image:F1.large.jpg|frame|none|alt=Alt text|Figure 2. Structure of an Arginine kinase in an unbound conformation]][[Image:3M10 bio r 500.jpg]] | ||
Figure 1a (Left). Structure of an arginine kinase in substrate-bound form Figure 1b (right). Structure of an AK in an unbound conformation. | Figure 1a (Left). Structure of an arginine kinase in substrate-bound form Figure 1b (right). Structure of an AK in an unbound conformation. | ||
