Severin: Difference between revisions
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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. | [[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. | ||
*<scene name='41/410299/Cv/ | *<scene name='41/410299/Cv/9'>Ca coordination site</scene>. Water molecules are shown as red spheres. | ||
*<scene name='41/410299/Cv/10'>Na coordination site</scene>. | |||
</StructureSection> | </StructureSection> | ||
== 3D Structures of Severin == | == 3D Structures of Severin == | ||
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | |||
[[3fg6]] – Adseverin C-terminal – human<br /> | [[3fg6]] – Adseverin C-terminal – human<br /> | ||
[[1svy]] – DdSeverin domain 2 – ''Dictyostelium discoideum'' <br /> | [[1svy]] – DdSeverin domain 2 – ''Dictyostelium discoideum'' <br /> |
Latest revision as of 13:26, 19 November 2023
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.
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3D Structures of Severin3D Structures of Severin
Updated on 19-November-2023
3fg6 – Adseverin C-terminal – human
1svy – DdSeverin domain 2 – Dictyostelium discoideum
1svq, 1svr - DdSeverin domain 2 - NMR
ReferencesReferences
- ↑ 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