Caspase
From Proteopedia
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[[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 /> | ||
Revision as of 08:17, 20 January 2020
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References
- ↑ Schweizer A, Briand C, Grutter MG. Crystal structure of caspase-2, apical initiator of the intrinsic apoptotic pathway. J Biol Chem. 2003 Oct 24;278(43):42441-7. Epub 2003 Aug 14. PMID:12920126 doi:http://dx.doi.org/10.1074/jbc.M304895200
- ↑ Wilson KP, Black JA, Thomson JA, Kim EE, Griffith JP, Navia MA, Murcko MA, Chambers SP, Aldape RA, Raybuck SA, et al.. Structure and mechanism of interleukin-1 beta converting enzyme. Nature. 1994 Jul 28;370(6487):270-5. PMID:8035875 doi:http://dx.doi.org/10.1038/370270a0
