User:Michael Adams/Sandbox 1: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 11: | Line 11: | ||
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 <scene name='71/716599/Mynewscene/1'>α-helices</scene> 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 <scene name='71/716599/Mynewscene/1'>α-helices</scene> flanking the sheet (Figure 1). | ||
[[Image:F1.large.jpg|frame|none|alt=Alt text|Figure 1. Structure of an AK in substrate-bound form]][[Image:3M10 bio r 500.jpg|frame|none|alt=Alt text|Figure 2. Structure of an AK in an unbound conformation]] | |||
