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Destrin

From Wikipedia, the free encyclopedia
Protein found in humans
Destrin (actin binding protein)
Nuclear magnetic resonance determined configuration of the tertiary structure of Destrin.[1]
Identifiers
SymbolDSTN
Alt. symbolsADF
NCBI gene11034
HGNC15750
OMIM609114
RefSeqNM_006870
UniProtP60981
Other data
LocusChr. 20p12.1
Search for
StructuresSwiss-model
DomainsInterPro

Destrin orDSTN (also known asactin depolymerizing factor orADF) is aprotein which in humans is encoded by theDSTNgene.[2][3][4] Destrin is a component protein inmicrofilaments.

The product of this gene belongs to theactin-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

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The tertiary structure of destrin was determined by the use of triple-resonance multidimensional nuclear magnetic resonance, orNMR for short.[1] The secondary and tertiary structures of destrin are similar to thegelsolin family which is another actin-regulating protein family.

There are three ordered layers to destrin which is a globular protein. There is a centralβ sheet that is composed of one parallel strand and three antiparallel strands. This β sheet is between a longα 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

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In a variety ofeukaryotes, 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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  1. ^abcdPDB: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.
  2. ^ab"Entrez Gene: Destrin".
  3. ^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.
  4. ^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]
Human
Microfilaments
andABPs
Myofilament
Actins
Myosins
Other
Other
Intermediate
filaments
Type 1/2
(Keratin,
Cytokeratin)
Epithelial keratins
(soft alpha-keratins)
Hair keratins
(hard alpha-keratins)
Ungrouped alpha
Not alpha
Type 3
Type 4
Type 5
Microtubules
andMAPs
Tubulins
MAPs
Kinesins
Dyneins
Microtubule organising proteins
Microtubule severing proteins
Other
Catenins
Membrane
Other
Nonhuman

This article incorporates text from theUnited States National Library of Medicine, which is in thepublic domain.

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