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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2004-7-27
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pubmed:databankReference |
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pubmed:abstractText |
Mutations in the Lis1 gene result in lissencephaly (smooth brain), a debilitating developmental syndrome caused by the impaired ability of postmitotic neurons to migrate to their correct destination in the cerebral cortex. Sequence similarities suggest that the LIS1 protein contains a C-terminal seven-blade beta-propeller domain, while the structure of the N-terminal fragment includes the LisH (Lis-homology) motif, a pattern found in over 100 eukaryotic proteins with a hitherto unknown function. We present the 1.75 A resolution crystal structure of the N-terminal domain of mouse LIS1, and we show that the LisH motif is a novel, thermodynamically very stable dimerization domain. The structure explains the molecular basis of a low severity form of lissencephaly.
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pubmed:grant |
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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 |
Jun
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pubmed:issn |
0969-2126
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
987-98
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:15274919-1-Alkyl-2-acetylglycerophosphocholine Esterase,
pubmed-meshheading:15274919-Amino Acid Motifs,
pubmed-meshheading:15274919-Amino Acid Sequence,
pubmed-meshheading:15274919-Animals,
pubmed-meshheading:15274919-Dimerization,
pubmed-meshheading:15274919-Dose-Response Relationship, Drug,
pubmed-meshheading:15274919-Guanidine,
pubmed-meshheading:15274919-Mice,
pubmed-meshheading:15274919-Microtubule-Associated Proteins,
pubmed-meshheading:15274919-Models, Molecular,
pubmed-meshheading:15274919-Molecular Sequence Data,
pubmed-meshheading:15274919-Mutation,
pubmed-meshheading:15274919-Protein Conformation,
pubmed-meshheading:15274919-Protein Denaturation,
pubmed-meshheading:15274919-Protein Folding,
pubmed-meshheading:15274919-Protein Structure, Secondary,
pubmed-meshheading:15274919-Protein Structure, Tertiary,
pubmed-meshheading:15274919-Sequence Homology, Amino Acid,
pubmed-meshheading:15274919-Thermodynamics
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pubmed:year |
2004
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pubmed:articleTitle |
The structure of the N-terminal domain of the product of the lissencephaly gene Lis1 and its functional implications.
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pubmed:affiliation |
Department of Molecular Physiology and Biological Physics and Cancer Center, University of Virginia, Charlottesville, VA 22908, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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