Sandbox Reserved 954: Difference between revisions

Structural studies on serpins revealed that inhibitory members of the family undergo an unusual conformational change, termed the Stressed to Relaxed (S to R) transition. During this structural transition the <scene name='60/604473/The_rcl_loop_scene/3'>RCL</scene> inserts into A β-sheet and forms an extra fourth β strand . The serpin conformational change is key to the mechanism of inhibition of target 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 efficient and rapid insertion of the RCL into the A β-sheet.<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>

The <scene name='60/604473/The_rcl_loop_scene/3'>RCL</scene> is cleaved at a scissile bond between two residues <scene name='60/604473/P1_scene/3'>Ser354 termed P1 (N-terminal of the cleavage event) and Ser355 termed P1’ (C-terminal of the cleavage event)</scene>. The P1 and P1' residues are critical for serpin specificity and mutation of these residues results in the loss or conversion of inhibitory activity. The protease recognize <scene name='60/604473/Amino_acids_for_protease_recog/1'>amino-acids of the RCL</scene> that allow its docking.