Caspase-7 - Revision history

Wu3857: /* Related Pathway */

2020-01-04T05:10:27Z

‎Related Pathway

Wu3857: /* Reference */

2020-01-04T04:56:00Z

‎Reference

Wu3857: /* Reference */

2020-01-04T04:55:40Z

‎Reference

Wu3857: /* Reference */

2020-01-04T04:55:06Z

‎Reference

Wu3857 at 04:54, 4 January 2020

2020-01-04T04:54:06Z

Wu3857: /* Protein Function */

2020-01-04T04:52:51Z

‎Protein Function

Wu3857: Created page with "{| align="left" | TOC |} {{#invoke:InfoboxforTarget|run|CASP7|[https://www.uniprot.org/uniprot/P55210 P55210]|Homo sapiens|Cys186|[http://pfam.xfam.org/family/PF00656..."

2020-01-04T04:51:49Z

Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|CASP7|[https://www.uniprot.org/uniprot/P55210 P55210]|Homo sapiens|Cys186|[http://pfam.xfam.org/family/PF00656..."

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{| align="left"
| __TOC__
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{{#invoke:InfoboxforTarget|run|CASP7|[https://www.uniprot.org/uniprot/P55210 P55210]|Homo sapiens|Cys186|[http://pfam.xfam.org/family/PF00656 Peptidase C14A family]|[[:Category:Caspase-7|Ligand list]]|Protease}}
==Summary==

===Protein Function ===
Caspases (cysteine-aspartic acid protease (Caspase) family) are a family of cysteine proteases that have important intracellular roles in inflammation and apoptosis. Activation of Caspases ensures that the cellular components are degraded in a controlled manner, carrying out cell death with minimal effect on surrounding tissues. Caspases exist as inactive proenzymes composed of a prodomain, a large protease subunit, and a small protease subunit. Activation of Caspases requires proteolytic processing at conserved internal aspartic residues to generate a heterodimeric enzyme consisting of the large and small subunits. 
Caspase-7 is a member of the Caspase (cysteine aspartate protease) family of proteins, and has been shown to be an executioner protein of apoptosis. Sequential activation of Caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes that undergo proteolytic processing by upstream Caspases (Caspase-8, -9) at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme in the form of a heterotetramer. The precursor of this Caspase is cleaved by Caspase 3, Caspase 10, and Caspase 9. It is activated upon cell death stimuli and induces apoptosis. Alternative splicing results in four transcript variants, encoding three distinct isoforms. (From Wikipedia) 
Involved in the activation cascade of Caspases responsible for apoptosis execution. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Overexpression promotes programmed cell death. (From Uniprot)
 

===Cys Function & Property===
The catalytic triad in Caspase-7 comprises Cys186, His144 and the backbone carbonyl oxygen atom of Arg87, which points towards the Nϵ atom of His144. 

* Hydrophobic property:
:[[File:593-hydro.png||600px]]
* SASA:
:Cys186: 14.133 A^2 

==Protein Sequence==

MADDQGCIEE QGVEDSANED SVDAKPDRSS FVPSLFSKKK KNVTMRSIKT 
TRDRVPTYQY NMNFEKLGKC IIINNKNFDK VTGMGVRNGT DKDAEALFKC 
FRSLGFDVIV YNDCSCAKMQ DLLKKASEED HTNAACFACI LLSHGEENVI 
YGKDGVTPIK DLTAHFRGDR CKTLLEKPKL FFIQA'''C'''RGTE LDDGIQADSG 
PINDTDANPR YKIPVEADFL FAYSTVPGYY SWRSPGRGSW FVQALCSILE 
EHGKDLEIMQ ILTRVNDRVA RHFESQSDDP HFHEKKQIPC VVSMLTKELY 
FSQ 


==Structural Information==
*Known structure with covalent ligand: 
:[https://www.rcsb.org/structure/1F1J 1F1J] 
:[https://www.rcsb.org/structure/3IBC 3IBC] 

*Protein structure:
[[File:593.png|center|800px]]

==Related Pathway==
*[https://www.genome.jp/kegg-bin/show_pathway?ko04210 Apoptosis] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko04215 Apoptosis - multiple species] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko04668 TNF signaling pathway] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko04932 Non-alcoholic fatty liver disease (NAFLD)] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko05010 Alzheimer disease] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko05130 Pathogenic Escherichia coli infection] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko05133 Pertussis] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko05134 Legionellosis] 
*[https://www.genome.jp/kegg-bin/show_pathway?ko05200 Pathways in cancer] 

==Experimental Evidence==
:Crystallography

==Reference==
# Agniswamy J, Fang B, Weber I T. '''Conformational similarity in the activation of caspase-3 and-7 revealed by the unliganded and inhibited structures of caspase-7[J].''' Apoptosis, 2009, 14(10): 1135-1144. [https://www.ncbi.nlm.nih.gov/pubmed/?term=19655253 19655253] 
# Y Wei, T Fox, S P Chambers et al. '''The structures of caspases-1, -3, -7 and -8 reveal the basis for substrate and inhibitor selectivity.''' Chem Biol, 2000, 7(6): 423-432. [https://www.ncbi.nlm.nih.gov/pubmed/?term=10873833 10873833] 

[[Category:Targets]]
[[Category:Homo sapiens]]
[[Category:Protease]]
[[Category:Peptidase C14A family]]
[[Category:Apoptosis]]
[[Category:Apoptosis - multiple species]]
[[Category:TNF signaling pathway]]
[[Category:Non-alcoholic fatty liver disease (NAFLD)]]
[[Category:Alzheimer disease]]
[[Category:Pathogenic Escherichia coli infection]]
[[Category:Pertussis]]
[[Category:Legionellosis]]
[[Category:Pathways in cancer]]

@@ Line 40: / Line 40: @@
 ==Related Pathway==
 *[https://www.genome.jp/kegg-bin/show_pathway?ko04210 Apoptosis]<br/>
 *[https://www.genome.jp/kegg-bin/show_pathway?ko04668 TNF signaling pathway]<br/>
 *[https://www.genome.jp/kegg-bin/show_pathway?ko04932 Non-alcoholic fatty liver disease (NAFLD)]<br/>
@@ Line 48: / Line 47: @@
 *[https://www.genome.jp/kegg-bin/show_pathway?ko05134 Legionellosis]<br/>
 *[https://www.genome.jp/kegg-bin/show_pathway?ko05200 Pathways in cancer]<br/>
 ==Experimental Evidence==

@@ Line 55: / Line 55: @@
 ==Reference==
 # Agniswamy J, Fang B, Weber I T. '''Conformational similarity in the activation of caspase-3 and-7 revealed by the unliganded and inhibited structures of caspase-7[J].''' Apoptosis, 2009, 14(10): 1135-1144. [https://www.ncbi.nlm.nih.gov/pubmed/?term=19655253 19655253]<br/>
-# Wei Y, Fox T, Chambers S P et al. '''The structures of caspases-1, -3, -7 and -8 reveal the basis for substrate and inhibitor selectivity.''' Chem Biol, 2000, 7(6): 423-432. [https://www.ncbi.nlm.nih.gov/pubmed/?term=10873833 10873833]<br/>
+# Wei Y, Fox T, Chambers S P et al. '''The structures of caspases-1, -3, -7 and -8 reveal the basis for substrate and inhibitor selectivity[J].''' Chem Biol, 2000, 7(6): 423-432. [https://www.ncbi.nlm.nih.gov/pubmed/?term=10873833 10873833]<br/>
 [[Category:Targets]]

@@ Line 55: / Line 55: @@
 ==Reference==
 # Agniswamy J, Fang B, Weber I T. '''Conformational similarity in the activation of caspase-3 and-7 revealed by the unliganded and inhibited structures of caspase-7[J].''' Apoptosis, 2009, 14(10): 1135-1144. [https://www.ncbi.nlm.nih.gov/pubmed/?term=19655253 19655253]<br/>
-# Y Wei, T Fox, S P Chambers et al. '''The structures of caspases-1, -3, -7 and -8 reveal the basis for substrate and inhibitor selectivity.''' Chem Biol, 2000, 7(6): 423-432. [https://www.ncbi.nlm.nih.gov/pubmed/?term=10873833 10873833]<br/>
+# Wei Y, Fox T, Chambers S P et al. '''The structures of caspases-1, -3, -7 and -8 reveal the basis for substrate and inhibitor selectivity.''' Chem Biol, 2000, 7(6): 423-432. [https://www.ncbi.nlm.nih.gov/pubmed/?term=10873833 10873833]<br/>
 [[Category:Targets]]

@@ Line 7: / Line 7: @@
 ===Protein Function ===
 Caspases (cysteine-aspartic acid protease (Caspase) family) are a family of cysteine proteases that have important intracellular roles in inflammation and apoptosis. Activation of Caspases ensures that the cellular components are degraded in a controlled manner, carrying out cell death with minimal effect on surrounding tissues. Caspases exist as inactive proenzymes composed of a prodomain, a large protease subunit, and a small protease subunit. Activation of Caspases requires proteolytic processing at conserved internal aspartic residues to generate a heterodimeric enzyme consisting of the large and small subunits. <br/> <br/>
-Caspase-7 is a member of the Caspase (cysteine aspartate protease) family of proteins, and has been shown to be an executioner protein of apoptosis. Sequential activation of Caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes that undergo proteolytic processing by upstream Caspases (Caspase-8, -9) at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme in the form of a heterotetramer. The precursor of this Caspase is cleaved by Caspase 3, Caspase 10, and Caspase 9. It is activated upon cell death stimuli and induces apoptosis. Alternative splicing results in four transcript variants, encoding three distinct isoforms. (From Wikipedia)<br/>
+Caspase-7 is a member of the Caspase family of proteins, and has been shown to be an executioner protein of apoptosis. Sequential activation of Caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes that undergo proteolytic processing by upstream Caspases (Caspase-8, -9) at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme in the form of a heterotetramer. The precursor of this Caspase is cleaved by Caspase 3, Caspase 10, and Caspase 9. It is activated upon cell death stimuli and induces apoptosis. Alternative splicing results in four transcript variants, encoding three distinct isoforms. (From Wikipedia)<br/>
 Involved in the activation cascade of Caspases responsible for apoptosis execution. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Overexpression promotes programmed cell death. (From Uniprot)
 <br/>

@@ Line 6: / Line 6: @@
 ===Protein Function ===
-Caspases (cysteine-aspartic acid protease (Caspase) family) are a family of cysteine proteases that have important intracellular roles in inflammation and apoptosis. Activation of Caspases ensures that the cellular components are degraded in a controlled manner, carrying out cell death with minimal effect on surrounding tissues. Caspases exist as inactive proenzymes composed of a prodomain, a large protease subunit, and a small protease subunit. Activation of Caspases requires proteolytic processing at conserved internal aspartic residues to generate a heterodimeric enzyme consisting of the large and small subunits. <br/>
+Caspases (cysteine-aspartic acid protease (Caspase) family) are a family of cysteine proteases that have important intracellular roles in inflammation and apoptosis. Activation of Caspases ensures that the cellular components are degraded in a controlled manner, carrying out cell death with minimal effect on surrounding tissues. Caspases exist as inactive proenzymes composed of a prodomain, a large protease subunit, and a small protease subunit. Activation of Caspases requires proteolytic processing at conserved internal aspartic residues to generate a heterodimeric enzyme consisting of the large and small subunits. <br/> <br/>
 Caspase-7 is a member of the Caspase (cysteine aspartate protease) family of proteins, and has been shown to be an executioner protein of apoptosis. Sequential activation of Caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes that undergo proteolytic processing by upstream Caspases (Caspase-8, -9) at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme in the form of a heterotetramer. The precursor of this Caspase is cleaved by Caspase 3, Caspase 10, and Caspase 9. It is activated upon cell death stimuli and induces apoptosis. Alternative splicing results in four transcript variants, encoding three distinct isoforms. (From Wikipedia)<br/>
 Involved in the activation cascade of Caspases responsible for apoptosis execution. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Overexpression promotes programmed cell death. (From Uniprot)

@@ Line 62: / Line 62: @@
 [[Category:Peptidase C14A family]]
 [[Category:Apoptosis]]
 [[Category:TNF signaling pathway]]
 [[Category:Non-alcoholic fatty liver disease (NAFLD)]]

Caspase-7 - Revision history

Wu3857: /* Related Pathway */

Wu3857: /* Reference */

Wu3857: /* Reference */

Wu3857: /* Reference */

Wu3857 at 04:54, 4 January 2020

Wu3857: /* Protein Function */

Wu3857: Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|CASP7|[https://www.uniprot.org/uniprot/P55210 P55210]|Homo sapiens|Cys186|[http://pfam.xfam.org/family/PF00656..."

Wu3857: Created page with "{| align="left" | TOC |} {{#invoke:InfoboxforTarget|run|CASP7|[https://www.uniprot.org/uniprot/P55210 P55210]|Homo sapiens|Cys186|[http://pfam.xfam.org/family/PF00656..."