Peroxiredoxin: Difference between revisions
Michal Harel (talk | contribs) No edit summary |
Michal Harel (talk | contribs) No edit summary |
||
(14 intermediate revisions by 3 users not shown) | |||
Line 1: | Line 1: | ||
<StructureSection load='1qq2' size='350' side='right' scene='43/433646/Cv/2' caption='Typical 2-cys peroxiredoxin dimer complex with Cl- ions [[1qq2]]'> | |||
== Function == | == Function == | ||
[[Peroxiredoxin]] (Prx) is an antioxidant enzyme. In the Prxs the active-site Cys is oxidized to sulfenic acid | [[Peroxiredoxin]] (Prx) is an antioxidant enzyme. In the Prxs the active-site Cys is oxidized to sulfenic acid hyper oxide forming a Cys-SOH intermediate. A second Cys residue resolves the intermediate to a protein disulfide bond. The Prxs are divided into 3 types according to their intermediate resolving mechanism: '''typical 2-Cysteine Prx''' in which the Cys-Cys bond is formed between two subunits, '''atypical 2-Cys Prx''' in which the bond is formed within one subunit and '''1-Cysteine Prx''' which uses a single Cys residue for the catalysis. '''Prx Q''' is the plant homolog of [[Bacterioferritin comigratory protein]]. | ||
'''Typical 2-Cys Prx'''<br /> | '''Typical 2-Cys Prx'''<br /> | ||
Line 9: | Line 9: | ||
* '''Prx 4''' localizes to the cytoplasm and regulates the activation of NF-κB<ref>PMID:25656995</ref>. | * '''Prx 4''' localizes to the cytoplasm and regulates the activation of NF-κB<ref>PMID:25656995</ref>. | ||
'''Atypical 2-Cys Prx'''<br /> | '''Atypical 2-Cys Prx'''<br /> | ||
* '''Prx 5''' | * '''Prx 5''' protects from mitochondrial DNA damage induced by H<sub>2</sub>O<sub>2</sub><ref>PMID:15848167</ref>. | ||
'''1-Cys Prx'''<br /> | '''1-Cys Prx'''<br /> | ||
* '''Prx 6''' | * '''Prx 6''' reduces peroxidized membrane phospholipids<ref>PMID:20919932</ref>. | ||
== Relevance == | == Relevance == | ||
Prx are over expressed in cancer tissue<ref>PMID:11497302</ref>. Prx 4 mediates osteoclast activation in cancer cells<ref>PMID:25779674</ref>. | Prx are over expressed in cancer tissue<ref>PMID:11497302</ref>. Prx 4 mediates osteoclast activation in cancer cells<ref>PMID:25779674</ref>. | ||
== Structural highlights == | |||
In the typical 2-cysteine Prx the <scene name='43/433646/Cv/5'>Cys-Cys bond is formed between two subunits</scene><ref>PMID:10535922</ref>. <scene name='43/433646/Cv/6'>Cl coordination site</scene>. Water molecules is shown as red sphere. | |||
== 3D Structures of Peroxiredoxin == | == 3D Structures of Peroxiredoxin == | ||
[[Peroxiredoxin 3D structures]] | |||
</StructureSection> | |||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] |