Severin

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{{STRUCTURE_1svy| PDB=1svy | SCENE= |CAPTION=Severin domain 2 complex with Ca+2 (green) and Na+ (purple) ions [[1svy]] }}
{{STRUCTURE_1svy| PDB=1svy | SCENE= |CAPTION=Severin domain 2 complex with Ca+2 (green) and Na+ (purple) ions [[1svy]] }}
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[[Severin]] is a calcium-activated protein which binds actin. The images at the top and at the right correspond to one representative severin structure, ''i.e.'' the human severin ([[3fg6]]). It nucleates actin assembly, severes F-actin and caps actin filaments. Severin is a member of the calcium-regulated gelsolin superfamily of actin severing and capping proteins. It is named Adseverin and Scinderin as well.
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[[Severin]] is a calcium-activated protein which binds actin. It nucleates actin assembly, severes F-actin and caps actin filaments. Severin is a member of the calcium-regulated gelsolin superfamily of actin severing and capping proteins<ref>PMID:15060630</ref>. It is named Adseverin and Scinderin as well.
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[[1svy]] – DdSeverin domain 2 – ''Dictyostelium discoideum'' <br />
[[1svy]] – DdSeverin domain 2 – ''Dictyostelium discoideum'' <br />
[[1svq]], [[1svr]] - DdSeverin domain 2 - NMR<br />
[[1svq]], [[1svr]] - DdSeverin domain 2 - NMR<br />
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 09:52, 28 August 2016

Crystal Structure of Human Severin, 3fg6
Crystal Structure of Human Severin, 3fg6

Template:STRUCTURE 1svy

Severin is a calcium-activated protein which binds actin. It nucleates actin assembly, severes F-actin and caps actin filaments. Severin is a member of the calcium-regulated gelsolin superfamily of actin severing and capping proteins[1]. It is named Adseverin and Scinderin as well.


3D Structures of Severin

3fg6 – Adseverin C-terminal – human
1svy – DdSeverin domain 2 – Dictyostelium discoideum
1svq, 1svr - DdSeverin domain 2 - NMR

References

  1. Summerscales J, Dawson JF. Probing Dictyostelium severin structure and function by cross linking to actin. Biochem Cell Biol. 2004 Apr;82(2):343-50. PMID:15060630 doi:http://dx.doi.org/10.1139/o04-002

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Alexander Berchansky, Michal Harel, Jaime Prilusky

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