| 词条 | Destrin |
| 释义 |
| Name = Destrin (actin binding protein) | caption = Nuclear magnetic resonance determined configuration of the tertiary structure of Destrin.[1] | image = Destrin.png | width = | HGNCid = 15750 | Symbol = DSTN | AltSymbols = ADF | EntrezGene = 11034 | OMIM = 609114 | RefSeq = NM_006870 | UniProt = P60981 | PDB = | ECnumber = | Chromosome = 20 | Arm = p | Band = 12.1 | LocusSupplementaryData = }} 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] StructureThe 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] FunctionIn 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] References1. ^1 2 3 {{PDB|1AK6}}; {{cite journal | vauthors = Hatanaka H, Ogura K, Moriyama K, Ichikawa S, Yahara I, Inagaki F | title = Tertiary structure of destrin and structural similarity between two actin-regulating protein families | journal = Cell | volume = 85 | issue = 7 | pages = 1047–55 |date=June 1996 | pmid = 8674111 | doi = 10.1016/S0092-8674(00)81305-7 | url = | issn = }} 2. ^1 {{cite web | title = Entrez Gene: Destrin | url =https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11034 | accessdate =}} 3. ^{{cite journal | vauthors = Hawkins M, Pope B, Maciver SK, Weeds AG | title = Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments | journal = Biochemistry | volume = 32 | issue = 38 | pages = 9985–93 |date=September 1993 | pmid = 8399167 | doi = 10.1021/bi00089a014| url = | issn = }} 4. ^{{cite journal | vauthors = Deloukas P, Matthews LH, Ashurst J | title = The DNA sequence and comparative analysis of human chromosome 20 | journal = Nature | volume = 414 | issue = 6866 | pages = 865–71 | year = 2001 | pmid = 11780052 | doi = 10.1038/414865a | url = | issn = |display-authors=etal}} External links
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