Structural highlights
Function
[DEST_HUMAN] Actin-depolymerizing protein. Severs actin filaments (F-actin) and binds to actin monomers (G-actin). Acts in a pH-independent manner.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Destrin is an isoprotein of cofilin that regulates actin cytoskeleton in various eukaryotes. We determined the tertiary structure of destrin by triple-resonance multidimensional nuclear magnetic resonance. In spite of there being no significant amino acid sequence homology, we found that the folding of destrin was strikingly similar to that of repeated segments in the gelsolin family, which resulted in a new protein fold group. Sequential dissimilarity of the actin-binding helix of destrin to that of gelsolin explains the Ca2+-independent actin-binding of destrin. Possible mechanisms of phosphorylation-sensitive phosphoinositide-competitive actin binding, of pH-dependent filament severing, and of nuclear translocation with actin in response to stresses, are discussed on the basis of the tertiary structure.
Tertiary structure of destrin and structural similarity between two actin-regulating protein families.,Hatanaka H, Ogura K, Moriyama K, Ichikawa S, Yahara I, Inagaki F Cell. 1996 Jun 28;85(7):1047-55. PMID:8674111[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hatanaka H, Ogura K, Moriyama K, Ichikawa S, Yahara I, Inagaki F. Tertiary structure of destrin and structural similarity between two actin-regulating protein families. Cell. 1996 Jun 28;85(7):1047-55. PMID:8674111
