Sandbox Reserved 954: Difference between revisions
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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> | 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> | ||
[[Image:Structure region.jpg|thumbnail|300px]] | [[Image:Structure region.jpg|center|thumbnail|300px|'''Key regions able to control and modulate the conformational change of RCL''']] | ||
==Function== | ==Function== | ||
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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> http://genome.cshlp.org/content/10/12/1845 | 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> http://genome.cshlp.org/content/10/12/1845 | ||
[[Image:fonction1.jpg|center|thumbnail|900px|'''Mecanism of cathepsin S-inhibition by serpin B3''']] | |||
Before the hydrolysis of the acyl-enzyme intermediate, the serpin rapidly undergoes from Stressed to Relaxed transition. The <scene name='60/604473/The_rcl_loop_scene/3'>RCL</scene> remains covalently attached to the protease, however the protease is moved from the top to the bottom of SCCA1. http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0104935 | Before the hydrolysis of the acyl-enzyme intermediate, the serpin rapidly undergoes from Stressed to Relaxed transition. The <scene name='60/604473/The_rcl_loop_scene/3'>RCL</scene> remains covalently attached to the protease, however the protease is moved from the top to the bottom of SCCA1. http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0104935 | ||
