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Destrin

Protein found in humans


Protein found in humans

FieldValue
NameDestrin (actin binding protein)
captionNuclear magnetic resonance determined configuration of the tertiary structure of Destrin.
imageDestrin.png
HGNCid15750
SymbolDSTN
AltSymbolsADF
EntrezGene11034
OMIM609114
RefSeqNM_006870
UniProtP60981
Chromosome20
Armp
Band12.1

Destrin or DSTN (also known as actin depolymerizing factor or ADF) is a protein which in humans is encoded by the DSTN gene. 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.

Structure

The tertiary structure of destrin was determined by the use of triple-resonance multidimensional nuclear magnetic resonance, or NMR for short. 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.

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.

References

References

  1. (June 1996). "Tertiary structure of destrin and structural similarity between two actin-regulating protein families". Cell.
  2. "Entrez Gene: Destrin".
  3. (September 1993). "Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments". Biochemistry.
  4. (2001). "The DNA sequence and comparative analysis of human chromosome 20". Nature.
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