Sandbox Reserved 954: Difference between revisions

The inhibitory members of serpin family undergo an unusual conformational change, the Stressed to Relaxed transition. This structural transition causes the <scene name='60/604473/The_rcl_loop_scene/3'>RCL</scene> insertion into <scene name='60/604473/A_beta_sheet/3'>A β-sheet</scene> thereby the <scene name='60/604473/The_rcl_loop_scene/3'>RCL</scene> forms an extra β strand . The serpin conformational change is essential for the inhibition mechanism of proteases. <scene name='60/604473/Rcl_insertion_into_beta_sheet/1'>Some amino-acids of RCL</scene> wich belong to a consensus sequence for inhibitory serpins are thought to permit the insertion of the <scene name='60/604473/The_rcl_loop_scene/3'>RCL</scene> into the <scene name='60/604473/A_beta_sheet/3'>A β-sheet</scene>.<ref> James C Whisstocka, 2, Richard Skinnera, 2, Robin W Carrella, Arthur M Leska, Conformational changes in serpins: I. the native and cleaved conformations of α1-antitrypsin1, http://www.sciencedirect.com/science/article/pii/S0022283699935209 DOI:pii/S0022283699935209</ref>

==Function==