Caspase: Difference between revisions

From Proteopedia
Jump to navigationJump to search
Michal Harel (talk | contribs)
No edit summary
Michal Harel (talk | contribs)
No edit summary
 
(2 intermediate revisions by the same user not shown)
Line 1: Line 1:
<StructureSection load='1pyo' size='350' side='right' scene='45/458455/Cv/1' caption='CASP-2 subunit P18 (purple, yellow) and subunit P12 (green, cyan) complex with polypeptide inhibitor (salmon, blue), aspartic aldehyde and acetyl group, [[1pyo]]'>
<StructureSection load='1pyo' size='350' side='right' scene='45/458455/Cv/1' caption='CASP-2 subunit P18 (purple, yellow) and subunit P12 (green, cyan) complex with polypeptide inhibitor (salmon, blue), aspartic aldehyde and acetyl group, [[1pyo]]'>


'''Caspase''' (CASP) are cysteine-aspartic proteases (see [[Protease]]) 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.<br />
'''Caspase''' (CASP) are cysteine-aspartic proteases (see [[Protease]]) 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.  The CASP recruitment domain (CARD) mediates signaling events that are associated with various human diseases including cancer, neuro-degenerative diseases and immune disorders<ref>PMID:30664151</ref>.<br />
*  '''CASP-1''' (or '''Interleukin-1 beta converting enzyme, ICE''') cleaves precursor cytokine interleukin 1-β and interleukin 18 into mature protein.  See:<br />
*  '''CASP-1''' (or '''Interleukin-1 beta converting enzyme, ICE''') cleaves precursor cytokine interleukin 1-β and interleukin 18 into mature protein.  See:<br />
[[Human Caspase-1]]<br />
[[Human Caspase-1]]<br />
Line 8: Line 8:
[[Student Projects for UMass Chemistry 423 Spring 2012-5]]<br />
[[Student Projects for UMass Chemistry 423 Spring 2012-5]]<br />
[[Caspase-3 Regulatory Mechanisms]]<br />
[[Caspase-3 Regulatory Mechanisms]]<br />
*  '''CASP-4''' binds the lipid moiety of lipopolysaccharide to induce the activation of non-canonical inflammasome<ref>PMID:29339744</ref>.<br/>
*  '''CASP-6''' is involved in the activation of cascade of caspases during apoptosis.  See:<br/>
*  '''CASP-6''' is involved in the activation of cascade of caspases during apoptosis.  See:<br/>
[[Molecular Playground/Caspase-6 (new)]]<br />
[[Molecular Playground/Caspase-6 (new)]]<br />
[[Caspase-6 and neurodegeneration]]<br />
[[Caspase-6 and neurodegeneration]]<br />
*  '''CASP-7''' is a heterodimer consisting of P20 (human residues 1-198) and P11 (human residues 199-303) subunits.  CASP-7 catalytic domain consists of residues 57-303. is an important initiator CASP and drICE is an effector of apoptosis CASP in ''Drosophila melanogaster''.  See:<br /> [[Molecular Playground/Caspase-7 Dynamics]]<br />
*  '''CASP-7''' is a heterodimer consisting of P20 (human residues 1-198) and P11 (human residues 199-303) subunits.  CASP-7 catalytic domain consists of residues 57-303. is an important initiator CASP and drICE is an effector of apoptosis CASP in ''Drosophila melanogaster''.  See:<br />
[[Molecular Playground/Caspase-7 Dynamics]]<br />
[[Molecular Playground/Executioner Caspase-7]]<br />
[[Molecular Playground/Executioner Caspase-7]]<br />
*  '''CASP-9''' is an aspartic protease linked to mitochondrial death pathway.  See:<br />
*  '''CASP-9''' is an aspartic protease linked to mitochondrial death pathway.  See:<br />

Latest revision as of 08:33, 30 May 2021

CASP-2 subunit P18 (purple, yellow) and subunit P12 (green, cyan) complex with polypeptide inhibitor (salmon, blue), aspartic aldehyde and acetyl group, 1pyo

Drag the structure with the mouse to rotate

References

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky