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Destrin (actin binding protein)
Destrin.png
Nuclear magnetic resonance determined configuration of the tertiary structure of Destrin.[1]
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]

Contents

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 segement-1 does. Furthermore, the binding of actin by destrin and cofilin is regulated negatively by phosphorylation. Destrin can also sever actin filaments. At a pH of 7.3 or higher it can sever the filaments but a lower pH the ability for it to do so is limited.[1]

References

  1. ^ 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.  
  2. ^ a b "Entrez Gene: Destrin". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11034.  
  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. 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. doi:10.1038/414865a. PMID 11780052.  

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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