Severin: Difference between revisions

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<StructureSection load='1svy' size='350' side='right' scene='' caption='Severin domain 2 complex with Ca+2 (green) and Na+ (purple) ions [[1svy]]'>
[[Image:Severin.png|left|200px|thumb|Crystal Structure of Human Severin, [[3fg6]]]]
[[Image:Severin.png|left|200px|thumb|Crystal Structure of Human Severin, [[3fg6]]]]
{{STRUCTURE_1svy| PDB=1svy  |  SCENE= |CAPTION=Severin domain 2 complex with Ca+2 (green) and Na+ (purple) ions [[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<ref>PMID:15060630</ref>. It is named Adseverin and Scinderin as well.   
[[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.   


 
</StructureSection>


== 3D Structures of Severin ==
== 3D Structures of Severin ==

Revision as of 12:54, 28 May 2017

Crystal Structure of Human Severin, 3fg6

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.


Severin domain 2 complex with Ca+2 (green) and Na+ (purple) ions 1svy

Drag the structure with the mouse to rotate

3D Structures of Severin3D Structures of Severin

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

ReferencesReferences

  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