Destrin
Destrin (actin binding protein) | |
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File:Destrin.png
Nuclear magnetic resonance determined configuration of the tertiary structure of Destrin.[1]
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Identifiers | |
Symbol | DSTN |
Alt. symbols | ADF |
Entrez | 11034 |
HUGO | 15750 |
OMIM | 609114 |
RefSeq | NM_006870 |
UniProt | P60981 |
Other data | |
Locus | Chr. 20 p12.1 |
Destrin or DSTN (also known as actin depolymerizing factor or ADF) is a protein which in humans is encoded by the DSTN gene.[2][3][4] Destrin is a component protein in microfilaments.
The product of this gene belongs to the actin-binding proteins ADF (Actin-Depolymerizing Factor)/cofilin family. This family of proteins is responsible for enhancing the turnover rate of actin in vivo. This gene encodes the actin depolymerizing protein that severs actin filaments (F-actin) and binds to actin monomers (G-actin). Two transcript variants encoding distinct isoforms have been identified for this gene.[2]
Structure
The tertiary structure of destrin was determined by the use of triple-resonance multidimensional nuclear magnetic resonance, NMR.[1] The secondary and tertiary structures of destrin are similar to the gelsolin family which is another actin-regulating protein family.
There are three ordered layers to destrin which is a globular protein. There is a central β sheet that is composed of one parallel strand and three antiparallel strands. This β sheet is between a long α helix along with a shorter one and two shorter helices on the opposite side. The four helices are parallel to the β strands.[1]
Function
In a variety of eukaryotes, destrin regulates actin in the cytoskeleton. Destrin binds actin and is thought to connect it as gelsolin segment-1 does. Furthermore, the binding of actin by destrin and cofilin is regulated negatively by phosphorylation. Destrin can also sever actin filaments. [1]
References
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External links
- Destrin at the US National Library of Medicine Medical Subject Headings (MeSH)
- Ramachandran Plot for destrin: Lua error in package.lua at line 80: module 'strict' not found.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.