Sandbox Reserved 954: Difference between revisions

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The <scene name='60/604473/The_rcl_loop_scene/3'>RCL</scene> of a serpin acts as a substrate for its cognate protease. 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 <scene name='60/604473/The_rcl_loop_scene/3'>RCL</scene> of a serpin acts as a substrate for its cognate protease. The protease recognize <scene name='60/604473/Amino_acids_for_protease_recog/1'>amino-acids of the RCL</scene> that allow its docking. 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.

<ref>M. S. J. Mangan, D. Kaiserman & P. I. Bird, The role of serpins in vertebrate immunity

Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria, Australiahttp://onlinelibrary.wiley.com/doi/10.1111/j.1399-0039.2008.01059.x/pdf DOI : 10.1111/j.1399-0039.2008.01059.x/pdf </ref>

Sandbox Reserved 954: Difference between revisions

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@@ Line 48: / Line 48: @@
-The <scene name='60/604473/The_rcl_loop_scene/3'>RCL</scene> of a serpin acts as a substrate for its cognate protease. 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 <scene name='60/604473/The_rcl_loop_scene/3'>RCL</scene> of a serpin acts as a substrate for its cognate protease. The protease recognize <scene name='60/604473/Amino_acids_for_protease_recog/1'>amino-acids of the RCL</scene> that allow its docking. 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.
 <ref>M. S. J. Mangan, D. Kaiserman & P. I. Bird, The role of serpins in vertebrate immunity
 Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria, Australiahttp://onlinelibrary.wiley.com/doi/10.1111/j.1399-0039.2008.01059.x/pdf DOI : 10.1111/j.1399-0039.2008.01059.x/pdf </ref>