Caspase-3/Sandbox: Difference between revisions

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====Active Site/Ligand Binding====

This is a morph of caspase-3 from its uninhibited form ~~([[1qx3]])~~ to inhibition ~~([[3kjf]])~~ by novel irreversible inhibitor B92 ((3S)-3-({[(5S,10aS)-2-{(2S)-4-carboxy-2-[(phenylacetyl)amino]butyl}-1,3-dioxo-2,3,5,7,8,9,10,10a-octahydro-1H-[1,2,4]triazolo[1,2-a]cinnolin-5-yl]carbonyl}amino)-4-oxopentanoic acid~~)(<scene name='Caspase-3/Sandbox/Caspase_3_inhibition_morph/3'>restore initial scene</scene>~~). The <scene name='Caspase-3/Sandbox/Caspase_3_inhibition_morph/9'>active site of caspase-3 binding to inhibitor B92</scene> involves<scene name='Caspase-3/Sandbox/Caspase_3_inhibition_morph/12'>Gly121, Arg64, Gln161, Arg207, Ser205</scene>, and <scene name='Caspase-3/Sandbox/Caspase_3_inhibition_morph/13'>catalytic residue, Cys163</scene>. (Wang, Watt et al. 2010)

This is a morph <scene name='Caspase-3/Sandbox/Caspase_3_inhibition_morph/3'>1qx3 to 3kjf</scene> of caspase-3 from its uninhibited form to inhibition by novel irreversible inhibitor B92 ((3S)-3-({[(5S,10aS)-2-{(2S)-4-carboxy-2-[(phenylacetyl)amino]butyl}-1,3-dioxo-2,3,5,7,8,9,10,10a-octahydro-1H-[1,2,4]triazolo[1,2-a]cinnolin-5-yl]carbonyl}amino)-4-oxopentanoic acid). The <scene name='Caspase-3/Sandbox/Caspase_3_inhibition_morph/9'>active site of caspase-3 binding to inhibitor B92</scene> involves<scene name='Caspase-3/Sandbox/Caspase_3_inhibition_morph/12'>Gly121, Arg64, Gln161, Arg207, Ser205</scene>, and <scene name='Caspase-3/Sandbox/Caspase_3_inhibition_morph/13'>catalytic residue, Cys163</scene>. (Wang, Watt et al. 2010)

When cleaved into its active form, caspase-3 is then able to bind to its substrates via recognition of DEVD consensus sequence. Caspase-3, using its active site cysteine residue, is then able to cleave the substrate at the Asp residue occupying the P4 portion of the active site. This is a <scene name='Caspase-3/Sandbox/1qx3_2cjxv2_zdevdcmk/1'>morph</scene>([[1qx3]] to [[2cjx]])showing the binding of modified DEVD substrate (zDEVD-cmk) to the active site of caspase-3.

Caspase-3/Sandbox: Difference between revisions

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 ====Active Site/Ligand Binding====
 <StructureSection applet load=1qx3.3kjf.morph.pdb' size='400' side='right' caption='Morph showing conformational changes between unbound and inhibitor bound ' scene='Caspase-3/Sandbox/Caspase_3_inhibition_morph/3'>
-This is a morph of caspase-3 from its uninhibited form ([[1qx3]]) to inhibition ([[3kjf]]) by novel irreversible inhibitor B92 ((3S)-3-({[(5S,10aS)-2-{(2S)-4-carboxy-2-[(phenylacetyl)amino]butyl}-1,3-dioxo-2,3,5,7,8,9,10,10a-octahydro-1H-[1,2,4]triazolo[1,2-a]cinnolin-5-yl]carbonyl}amino)-4-oxopentanoic acid)(<scene name='Caspase-3/Sandbox/Caspase_3_inhibition_morph/3'>restore initial scene</scene>).  The <scene name='Caspase-3/Sandbox/Caspase_3_inhibition_morph/9'>active site of caspase-3 binding to inhibitor B92</scene> involves<scene name='Caspase-3/Sandbox/Caspase_3_inhibition_morph/12'>Gly121, Arg64, Gln161, Arg207, Ser205</scene>, and <scene name='Caspase-3/Sandbox/Caspase_3_inhibition_morph/13'>catalytic residue, Cys163</scene>. (Wang, Watt et al. 2010)
+This is a morph <scene name='Caspase-3/Sandbox/Caspase_3_inhibition_morph/3'>1qx3 to 3kjf</scene> of caspase-3 from its uninhibited form  to inhibition  by novel irreversible inhibitor B92 ((3S)-3-({[(5S,10aS)-2-{(2S)-4-carboxy-2-[(phenylacetyl)amino]butyl}-1,3-dioxo-2,3,5,7,8,9,10,10a-octahydro-1H-[1,2,4]triazolo[1,2-a]cinnolin-5-yl]carbonyl}amino)-4-oxopentanoic acid).  The <scene name='Caspase-3/Sandbox/Caspase_3_inhibition_morph/9'>active site of caspase-3 binding to inhibitor B92</scene> involves<scene name='Caspase-3/Sandbox/Caspase_3_inhibition_morph/12'>Gly121, Arg64, Gln161, Arg207, Ser205</scene>, and <scene name='Caspase-3/Sandbox/Caspase_3_inhibition_morph/13'>catalytic residue, Cys163</scene>. (Wang, Watt et al. 2010)
 When cleaved into its active form, caspase-3 is then able to bind to its substrates via recognition of DEVD consensus sequence. Caspase-3, using its active site cysteine residue, is then able to cleave the substrate at the Asp residue occupying the P4 portion of the active site. This is a <scene name='Caspase-3/Sandbox/1qx3_2cjxv2_zdevdcmk/1'>morph</scene>([[1qx3]] to [[2cjx]])showing the binding of modified DEVD substrate (zDEVD-cmk) to the active site of caspase-3.