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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
2003-4-25
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pubmed:databankReference |
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pubmed:abstractText |
The doublecortin-like domains (DCX), which typically occur in tandem, are novel microtubule-binding modules. DCX tandems are found in doublecortin, a 360-residue protein expressed in migrating neurons; the doublecortin-like kinase (DCLK); the product of the RP1 gene that is responsible for a form of inherited blindness; and several other proteins. Mutations in the gene encoding doublecortin cause lissencephaly in males and the 'double-cortex syndrome' in females. We here report a solution structure of the N-terminal DCX domain of human doublecortin and a 1.5 A resolution crystal structure of the equivalent domain from human DCLK. Both show a stable, ubiquitin-like tertiary fold with distinct structural similarities to GTPase-binding domains. We also show that the C-terminal DCX domains of both proteins are only partially folded. In functional assays, the N-terminal DCX domain of doublecortin binds only to assembled microtubules, whereas the C-terminal domain binds to both microtubules and unpolymerized tubulin.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1072-8368
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pubmed:author |
pubmed-author:BushwellerJohn HJH,
pubmed-author:CierpickiTomaszT,
pubmed-author:DauterZbigniewZ,
pubmed-author:DerewendaUrszulaU,
pubmed-author:DerewendaZygmunt SZS,
pubmed-author:DevedjievYanchoY,
pubmed-author:FengYuanyiY,
pubmed-author:KimMyung HeeMH,
pubmed-author:KrowarschDanielD,
pubmed-author:OtlewskiJacekJ,
pubmed-author:WalshChristopher ACA
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pubmed:issnType |
Print
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pubmed:volume |
10
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
324-33
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:12692530-Amino Acid Sequence,
pubmed-meshheading:12692530-Binding Sites,
pubmed-meshheading:12692530-Brain,
pubmed-meshheading:12692530-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:12692530-Conserved Sequence,
pubmed-meshheading:12692530-Humans,
pubmed-meshheading:12692530-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:12692530-Male,
pubmed-meshheading:12692530-Microtubule-Associated Proteins,
pubmed-meshheading:12692530-Microtubules,
pubmed-meshheading:12692530-Models, Molecular,
pubmed-meshheading:12692530-Molecular Sequence Data,
pubmed-meshheading:12692530-Mutation,
pubmed-meshheading:12692530-Nerve Tissue Proteins,
pubmed-meshheading:12692530-Neuropeptides,
pubmed-meshheading:12692530-Phosphoproteins,
pubmed-meshheading:12692530-Protein Conformation,
pubmed-meshheading:12692530-Protein-Serine-Threonine Kinases,
pubmed-meshheading:12692530-Sequence Alignment,
pubmed-meshheading:12692530-Sequence Homology, Amino Acid
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pubmed:year |
2003
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pubmed:articleTitle |
The DCX-domain tandems of doublecortin and doublecortin-like kinase.
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pubmed:affiliation |
Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia 22908-0736, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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