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.
| Destrin (actin binding protein) | |||||||
|---|---|---|---|---|---|---|---|
 Nuclear magnetic resonance determined configuration of the tertiary structure of Destrin.[1] | |||||||
| Identifiers | |||||||
| Symbol | DSTN | ||||||
| Alt. symbols | ADF | ||||||
| NCBI gene | 11034 | ||||||
| HGNC | 15750 | ||||||
| OMIM | 609114 | ||||||
| RefSeq | NM_006870 | ||||||
| UniProt | P60981 | ||||||
| Other data | |||||||
| Locus | Chr. 20 p12.1 | ||||||
| |||||||
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
editThe tertiary structure of destrin was determined by the use of triple-resonance multidimensional nuclear magnetic resonance, or NMR for short.[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
editIn 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
edit- ^ a b c d PDB: 1AK6; Hatanaka H, Ogura K, Moriyama K, Ichikawa S, Yahara I, Inagaki F (June 1996). "Tertiary structure of destrin and structural similarity between two actin-regulating protein families". Cell. 85 (7): 1047–55. doi:10.1016/S0092-8674(00)81305-7. PMID 8674111. S2CID 11470231.
- ^ a b "Entrez Gene: Destrin".
- ^ Hawkins M, Pope B, Maciver SK, Weeds AG (September 1993). "Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments". Biochemistry. 32 (38): 9985–93. doi:10.1021/bi00089a014. PMID 8399167.
- ^ Deloukas P, Matthews LH, Ashurst J, et al. (2001). "The DNA sequence and comparative analysis of human chromosome 20". Nature. 414 (6866): 865–71. Bibcode:2001Natur.414..865D. doi:10.1038/414865a. PMID 11780052.
External links
edit- Destrin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- Ramachandran Plot for destrin: "MolProbity Ramachandran analysis for 1ak6" (PDF). www.rcsb.org. Archived from the original (PDF) on 2012-10-12.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.