| 词条 | DM domain |
| 释义 |
| Symbol = DM | Name = DM domain | image = PDB 1lpv EBI.jpg | width = | caption = Drosophila melanogaster doublesex (dsx), nmr, 18 structures | Pfam = PF00751 | Pfam_clan = | SMART = SM00718 | PROSITE = | MEROPS = | SCOP = 1rvv | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = | InterPro = IPR001275 }} In molecular biology the DM domain is a protein domain first discovered in the doublesex proteins of Drosophila melanogaster and is also seen in proteins from Caenorhabditis elegans.[1] In D. melanogaster the doublesex gene controls somatic sexual differentiation by producing alternatively spliced mRNAs encoding related sex-specific polypeptides.[2] These proteins are believed to function as transcription factors on downstream sex-determination genes, especially on neuroblast differentiation and yolk protein genes transcription.[3][4] The DM domain binds DNA as a dimer, allowing the recognition of pseudopalindromic sequences .[2][5][6] The NMR analysis of the DSX DM domain [6] revealed a novel zinc module containing 'intertwined' CCHC and HCCC zinc-binding sites. The recognition of the DNA requires the carboxy-terminal basic tail which contacts the minor groove of the target sequence. References1. ^{{cite journal |vauthors=Raymond CS, Shamu CE, Shen MM, Seifert KJ, Hirsch B, Hodgkin J, Zarkower D | title = Evidence for evolutionary conservation of sex-determining genes | journal = Nature | volume = 391 | issue = 6668 | pages = 691–5 |date=February 1998 | pmid = 9490411 | doi = 10.1038/35618 | url = }} {{InterPro content|IPR001275}}2. ^1 {{cite journal |vauthors=Erdman SE, Chen HJ, Burtis KC | title = Functional and genetic characterization of the oligomerization and DNA binding properties of the Drosophila doublesex proteins | journal = Genetics | volume = 144 | issue = 4 | pages = 1639–52 |date=December 1996 | pmid = 8978051 | pmc = 1207715 | doi = | url = }} 3. ^{{cite journal|authorlink3=Bruce Baker (geneticist) |vauthors=Burtis KC, Coschigano KT, Baker BS, Wensink PC | title = The doublesex proteins of Drosophila melanogaster bind directly to a sex-specific yolk protein gene enhancer | journal = EMBO J. | volume = 10 | issue = 9 | pages = 2577–82 |date=September 1991 | pmid = 1907913 | pmc = 452955 | doi = | url = }} 4. ^{{cite journal |vauthors=Shen MM, Hodgkin J | title = mab-3, a gene required for sex-specific yolk protein expression and a male-specific lineage in C. elegans | journal = Cell | volume = 54 | issue = 7 | pages = 1019–31 |date=September 1988 | pmid = 3046751 | doi = 10.1016/0092-8674(88)90117-1| url = }} 5. ^{{cite journal |vauthors=Yi W, Zarkower D | title = Similarity of DNA binding and transcriptional regulation by Caenorhabditis elegans MAB-3 and Drosophila melanogaster DSX suggests conservation of sex determining mechanisms | journal = Development | volume = 126 | issue = 5 | pages = 873–81 |date=February 1999 | pmid = 9927589 | doi = | url = }} 6. ^1 {{cite journal |vauthors=Zhu L, Wilken J, Phillips NB, Narendra U, Chan G, Stratton SM, Kent SB, Weiss MA | title = Sexual dimorphism in diverse metazoans is regulated by a novel class of intertwined zinc fingers | journal = Genes Dev. | volume = 14 | issue = 14 | pages = 1750–64 |date=July 2000 | pmid = 10898790 | pmc = 316782 | doi = | url = }} 2 : Protein families|Protein domains |
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