User:Michael Adams/Sandbox 1: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 10: | Line 10: | ||
== Structure == | == Structure == | ||
The structure of <scene name='71/716599/My3/1'>arginine kinase</scene> is mainly α-helical and contains an N-terminal region with a specificity loop for specific substrate binding. (Figure 2). 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 <scene name='71/716599/Beta/1'>β-sheet</scene> with seven <scene name='71/716599/Mynewscene/1'>α-helices</scene> flanking the sheet (Figure 1). | The structure of <scene name='71/716599/My3/1'>arginine kinase</scene> is mainly α-helical and contains an N-terminal region with a specificity loop for specific substrate binding. (Figure 2). 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 <scene name='71/716599/Beta/1'>β-sheet</scene> with seven <scene name='71/716599/Mynewscene/1'>α-helices</scene> flanking the sheet (Figure 1). | ||
[[Image:F1.large.jpg|left|frame|none|alt=Alt text|Figure 1. Structure of an AK in substrate-bound form]] | [[Image:F1.large.jpg|left|frame|none|alt=Alt text|Figure 1. Structure of an AK in substrate-bound form]] | ||
