Caspase: Difference between revisions

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{{STRUCTURE_3d6f| PDB=3d6f | SIZE=400| SCENE= |right| CAPTION=CASP-1 complex with polypeptide inhibitor, benzyl chlorocarbonate and fluoro methane, [[3d6f]] }}

'''Caspase''' (CASP) are cysteine-aspartic proteases which function in apoptosis, necrosis and inflammation. Twelve CASP have been identified in human. CASP is synthesized as an inactive pro-CASP with a prodomain which is being cleaved off to render them active. The X-linked inhibitor of apoptosis protein (XIAP) with its baculoviral IAP repeat (BIR) domain is an inhibitor of CASP. CASP-1 cleaves precursor cytokine interleukin 1-β and interleukin 18 into mature protein. CASP-3 interacts with CASP-8 and CASP-9 during cell apoptosis. CASP-6 details in [[Molecular Playground/Caspase-6 (new)]]. CASP-7 details in [[Molecular Playground/Caspase-7 Dynamics]]. CASP-9 details in [[Molecular Playground/Caspase-9 Regulation]].

'''Caspase''' (CASP) are cysteine-aspartic proteases which function in apoptosis, necrosis and inflammation. Twelve CASP have been identified in human. CASP is synthesized as an inactive pro-CASP with a prodomain which is being cleaved off to render them active. The X-linked inhibitor of apoptosis protein (XIAP) with its baculoviral IAP repeat (BIR) domain is an inhibitor of CASP. CASP-1 cleaves precursor cytokine interleukin 1-β and interleukin 18 into mature protein. CASP-3 interacts with CASP-8 and CASP-9 during cell apoptosis. CASP-1 details in [[Human Caspase-1]]. CASP-6 details in [[Molecular Playground/Caspase-6 (new)]]. CASP-7 details in [[Molecular Playground/Caspase-7 Dynamics]]. CASP-9 details in [[Molecular Playground/Caspase-9 Regulation]].

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-  {{STRUCTURE_3d6f|  PDB=3d6f  | SIZE=300| SCENE= |right|   CAPTION=CASP-1 complex with polypeptide inhibitor, benzyl chlorocarbonate and fluoro methane, [[3d6f]] }}
+  {{STRUCTURE_3d6f|  PDB=3d6f  | SIZE=400| SCENE= |right|   CAPTION=CASP-1 complex with polypeptide inhibitor, benzyl chlorocarbonate and fluoro methane, [[3d6f]] }}
-'''Caspase''' (CASP) are cysteine-aspartic proteases which function in apoptosis, necrosis and inflammation.  Twelve CASP have been identified in human.  CASP is synthesized as an inactive pro-CASP with a prodomain which is being cleaved off to render them active.  The X-linked inhibitor of apoptosis protein (XIAP) with its baculoviral IAP repeat (BIR) domain is an inhibitor of CASP.  CASP-1 cleaves precursor cytokine interleukin 1-β and interleukin 18 into mature protein.  CASP-3 interacts with CASP-8 and CASP-9 during cell apoptosis.  CASP-6 details in [[Molecular Playground/Caspase-6 (new)]].  CASP-7 details in [[Molecular Playground/Caspase-7 Dynamics]].  CASP-9 details in [[Molecular Playground/Caspase-9 Regulation]].
+'''Caspase''' (CASP) are cysteine-aspartic proteases which function in apoptosis, necrosis and inflammation.  Twelve CASP have been identified in human.  CASP is synthesized as an inactive pro-CASP with a prodomain which is being cleaved off to render them active.  The X-linked inhibitor of apoptosis protein (XIAP) with its baculoviral IAP repeat (BIR) domain is an inhibitor of CASP.  CASP-1 cleaves precursor cytokine interleukin 1-β and interleukin 18 into mature protein.  CASP-3 interacts with CASP-8 and CASP-9 during cell apoptosis.  CASP-1 details in [[Human Caspase-1]].  CASP-6 details in [[Molecular Playground/Caspase-6 (new)]].  CASP-7 details in [[Molecular Playground/Caspase-7 Dynamics]].  CASP-9 details in [[Molecular Playground/Caspase-9 Regulation]].
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