Peroxiredoxin-4 - Revision history

Wu3857: /* Reference */

2019-08-19T23:09:55Z

‎Reference

Wu3857 at 01:39, 4 August 2019

2019-08-04T01:39:43Z

Wu3857 at 20:43, 29 July 2019

2019-07-29T20:43:12Z

Wu3857: /* Reference */

2019-07-28T20:25:20Z

‎Reference

Wu3857: /* Structural Information */

2019-07-28T18:17:41Z

‎Structural Information

Wu3857: /* Cys Function & Property */

2019-07-28T18:16:40Z

‎Cys Function & Property

Wu3857: /* Protein Function */

2019-07-28T18:16:25Z

‎Protein Function

Wu3857: /* Protein Function */

2019-07-28T18:16:05Z

‎Protein Function

Wu3857: /* Cys Function & Property */

2019-07-28T18:15:39Z

‎Cys Function & Property

Wu3857: Created page with "{| align="left" | TOC |} {{#invoke:InfoboxforTarget|run|PRDX4|[https://www.uniprot.org/uniprot/Q13162 Q13162]|Homo sapiens|Cys124, Cys245|[http://pfam.xfam.org/family/..."

2019-07-28T18:15:25Z

Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|PRDX4|[https://www.uniprot.org/uniprot/Q13162 Q13162]|Homo sapiens|Cys124, Cys245|[http://pfam.xfam.org/family/..."

New page

{| align="left"
| __TOC__
|}
{{#invoke:InfoboxforTarget|run|PRDX4|[https://www.uniprot.org/uniprot/Q13162 Q13162]|Homo sapiens|Cys124, Cys245|[http://pfam.xfam.org/family/PF00578 AhpC/TSA family], Peroxiredoxin family, AhpC/Prx1 subfamily|[[:Category:Peroxiredoxin-4|Ligand list]]}}
==Summary==

===Protein Function ===
Peroxiredoxin-4 belongs to the peroxiredoxin family. The protein is localized to the cytoplasm. Peroxidases of the peroxiredoxin family reduce hydrogen peroxide and alkyl hydroperoxides to water and alcohol with the use of reducing equivalents derived from thiol-containing donor molecules. This protein has been found to play a regulatory role in the activation of the transcription factor NF-kappaB. (From Wikipedia)
Peroxiredoxins provide antioxidant protection and act as signaling molecules and chaperones. Peroxiredoxins are widely conserved across eukaryotes. The active site of the “typical” class of peroxiredoxins is formed at the intersubunit interface of homodimers, which can assemble into rings of ten or twelve subunits. A catalytic peroxidatic cysteine residue reduces peroxide and other ROS, resulting in hyperoxidation to sulfenic (-SOH), sulfinic (-SO2H), or sulfonic acid (-SO3H) forms of the cysteine. The sulfenic acid form reacts with a second so-called resolving catalytic cysteine residue across the dimer interface to form an intermolecular disulfide bond. Oxidation to sulfinic acid can be repaired by sulfiredoxin, while the sulfonic acid form is considered irreversible. (PMID: 23891152)
 

===Cys Function & Property===
Cys124 is the active site of Peroxiredoxin-4. This redox-active residue is conserved in AhpC/TSA family. It considered as a peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. 
[[File:487-HMMlogo.png|center|800px]]
<div align="center">HMM logo of AphC/TSA family (N-terminal)</div> 

* Hydrophobic property:
:[[File:488-hydro.png||600px]]
* SASA：
:Cys124: 29.867
:Cys245: 26.577

==Protein Sequence==

MEALPLLAAT TPDHGRHRRL LLLPLLLFLL PAGAVQGWET EERPRTREEE 
CHFYAGGQVY PGEASRVSVA DHSLHLSKAK ISKPAPYWEG TAVIDGEFKE 
LKLTDYRGKY LVFFFYPLDF TFV'''C'''PTEIIA FGDRLEEFRS INTEVVACSV 
DSQFTHLAWI NTPRRQGGLG PIRIPLLSDL THQISKDYGV YLEDSGHTLR 
GLFIIDDKGI LRQITLNDLP VGRSVDETLR LVQAFQYTDK HGEV'''C'''PAGWK 
PGSETIIPDP AGKLKYFDKL N 


==Structural Information==
*Known structures with covalent ligands: 
:Unknown 

*Protein structure
[[File:488.png|center|800px]]

==Related Pathway==
*[https://www.genome.jp/kegg-bin/show_pathway?ko00480 Glutathione metabolism] 

==Experimental Evidence==
:Homologous Analysis of Sequence, Enzymatic Assay

==Reference==
# Nguyen J B, Pool C D, Wong C Y B, et al. '''Peroxiredoxin-1 from the human hookworm Ancylostoma ceylanicum forms a stable oxidized decamer and is covalently inhibited by conoidin A[J].''' Chemistry & Biology, 2013, 20(8): 991-1001. [https://www.ncbi.nlm.nih.gov/pubmed/?term=23891152 23891152] 

[[Category:Targets|Targets]]
[[Category:Peroxiredoxin family|Peroxiredoxin family]]
[[Category:AhpC/Prx1 subfamily|AhpC/Prx1 subfamily]]
[[Category:Glutathione metabolism|Glutathione metabolism]]

@@ Line 49: / Line 49: @@
-[[Category:Targets|Targets]]
+[[Category:Targets]]
-[[Category:Homo sapiens|Homo sapiens]]
+[[Category:Homo sapiens]]
-[[Category:Redox protein|Redox protein]]
+[[Category:Redox protein]]
-[[Category:Peroxiredoxin family|Peroxiredoxin family]]
+[[Category:Peroxiredoxin family]]
-[[Category:AhpC/Prx1 subfamily|AhpC/Prx1 subfamily]]
+[[Category:AhpC/Prx1 subfamily]]
-[[Category:Glutathione metabolism|Glutathione metabolism]]
+[[Category:Glutathione metabolism]]

@@ Line 35: / Line 35: @@
 :Unknown<br/>
-*Protein structure
+*Protein structure:
 [[File:488.png|center|800px]]

@@ Line 12: / Line 12: @@
 ===Cys Function & Property===
 Cys124 is the active site of Peroxiredoxin-4. This redox-active residue is conserved in AhpC/TSA family. It considered as a peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate.<br/><br/>
-[[File:487-HMMlogo.png|center|800px]]v
+[[File:487-HMMlogo.png|center|800px]]
 <div align="center">HMM logo of AphC/TSA family (N-terminal)</div><br/>

@@ Line 7: / Line 7: @@
 ===Protein Function ===
 Peroxiredoxin-4 belongs to the peroxiredoxin family. The protein is localized to the cytoplasm. Peroxidases of the peroxiredoxin family reduce hydrogen peroxide and alkyl hydroperoxides to water and alcohol with the use of reducing equivalents derived from thiol-containing donor molecules. This protein has been found to play a regulatory role in the activation of the transcription factor NF-kappaB. (From Wikipedia)<br/>
-Peroxiredoxins provide antioxidant protection and act as signaling molecules and chaperones. Peroxiredoxins are widely conserved across eukaryotes. The active site of the “typical” class of peroxiredoxins is formed at the intersubunit interface of homodimers, which can assemble into rings of ten or twelve subunits. A catalytic peroxidatic cysteine residue reduces peroxide and other ROS, resulting in hyperoxidation to sulfenic (-SOH), sulfinic (-SO2H), or sulfonic acid (-SO3H) forms of the cysteine. The sulfenic acid form reacts with a second so-called resolving catalytic cysteine residue across the dimer interface to form an intermolecular disulfide bond. Oxidation to sulfinic acid can be repaired by sulfiredoxin, while the sulfonic acid form is considered irreversible. (PMID: 23891152)
+Peroxiredoxins provide antioxidant protection and act as signaling molecules and chaperones. Peroxiredoxins are widely conserved across eukaryotes. The active site of the "typical" class of peroxiredoxins is formed at the intersubunit interface of homodimers, which can assemble into rings of ten or twelve subunits. A catalytic peroxidatic cysteine residue reduces peroxide and other ROS, resulting in hyperoxidation to sulfenic (-SOH), sulfinic (-SO2H), or sulfonic acid (-SO3H) forms of the cysteine. The sulfenic acid form reacts with a second so-called resolving catalytic cysteine residue across the dimer interface to form an intermolecular disulfide bond. Oxidation to sulfinic acid can be repaired by sulfiredoxin, while the sulfonic acid form is considered irreversible. (PMID: 23891152)
 <br/>

@@ Line 11: / Line 11: @@
 ===Cys Function & Property===
-Cys124 is the active site of Peroxiredoxin-4. This redox-active residue is conserved in AhpC/TSA family. It considered as a peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate.<br/>
+Cys124 is the active site of Peroxiredoxin-4. This redox-active residue is conserved in AhpC/TSA family. It considered as a peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate.<br/><br/>
-[[File:487-HMMlogo.png|center|800px]]
+[[File:487-HMMlogo.png|center|800px]]v
 <div align="center">HMM logo of AphC/TSA family (N-terminal)</div><br/>

@@ Line 2: / Line 2: @@
    | __TOC__
    |}
-{{#invoke:InfoboxforTarget|run|PRDX4|[https://www.uniprot.org/uniprot/Q13162 Q13162]|Homo sapiens|Cys124, Cys245|[http://pfam.xfam.org/family/PF00578 AhpC/TSA family], Peroxiredoxin family,<br/>AhpC/Prx1 subfamily|[[:Category:Peroxiredoxin-4|Ligand list]]|Antioxidant enzyme}}
+{{#invoke:InfoboxforTarget|run|PRDX4|[https://www.uniprot.org/uniprot/Q13162 Q13162]|Homo sapiens|Cys124, Cys245|[http://pfam.xfam.org/family/PF00578 AhpC/TSA family], Peroxiredoxin family,<br/>AhpC/Prx1 subfamily|[[:Category:Peroxiredoxin-4|Ligand list]]|Redox protein}}
 ==Summary==
@@ Line 51: / Line 51: @@
 [[Category:Targets|Targets]]
 [[Category:Homo sapiens|Homo sapiens]]
-[[Category:Antioxidant enzyme|Antioxidant enzyme]]
+[[Category:Redox protein|Redox protein]]
 [[Category:Peroxiredoxin family|Peroxiredoxin family]]
 [[Category:AhpC/Prx1 subfamily|AhpC/Prx1 subfamily]]
 [[Category:Glutathione metabolism|Glutathione metabolism]]

Peroxiredoxin-4 - Revision history

Wu3857: /* Reference */

Wu3857 at 01:39, 4 August 2019

Wu3857 at 20:43, 29 July 2019

Wu3857: /* Reference */

Wu3857: /* Structural Information */

Wu3857: /* Cys Function & Property */

Wu3857: /* Protein Function */

Wu3857: /* Protein Function */

Wu3857: /* Cys Function & Property */

Wu3857: Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|PRDX4|[https://www.uniprot.org/uniprot/Q13162 Q13162]|Homo sapiens|Cys124, Cys245|[http://pfam.xfam.org/family/..."

Wu3857: Created page with "{| align="left" | TOC |} {{#invoke:InfoboxforTarget|run|PRDX4|[https://www.uniprot.org/uniprot/Q13162 Q13162]|Homo sapiens|Cys124, Cys245|[http://pfam.xfam.org/family/..."