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rdf:type |
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lifeskim:mentions |
umls-concept:C0013352,
umls-concept:C0023693,
umls-concept:C0037633,
umls-concept:C0332281,
umls-concept:C0337112,
umls-concept:C0678594,
umls-concept:C1382100,
umls-concept:C1513492,
umls-concept:C1514562,
umls-concept:C1524075,
umls-concept:C1705994,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
7
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pubmed:dateCreated |
2000-7-21
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pubmed:databankReference |
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pubmed:abstractText |
Dyneins are molecular motors that translocate towards the minus ends of microtubules. In Chlamydomonas flagellar outer arm dynein, light chain 1 (LC1) associates with the nucleotide binding region within the gamma heavy chain motor domain and consists of a central leucine-rich repeat section that folds as a cylindrical right handed spiral formed from six beta-beta-alpha motifs. This central cylinder is flanked by terminal helical subdomains. The C-terminal helical domain juts out from the cylinder and is adjacent to a hydrophobic surface within the repeat region that is proposed to interact with the dynein heavy chain. The position of the C-terminal domain on LC1 and the unexpected structural similarity between LC1 and U2A' from the human spliceosome suggest that this domain interacts with the dynein motor domain.
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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 |
Jul
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pubmed:issn |
1072-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
575-9
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10876244-Amino Acid Motifs,
pubmed-meshheading:10876244-Amino Acid Sequence,
pubmed-meshheading:10876244-Animals,
pubmed-meshheading:10876244-Binding Sites,
pubmed-meshheading:10876244-Chlamydomonas reinhardtii,
pubmed-meshheading:10876244-Dyneins,
pubmed-meshheading:10876244-Flagella,
pubmed-meshheading:10876244-Humans,
pubmed-meshheading:10876244-Microtubule-Associated Proteins,
pubmed-meshheading:10876244-Models, Molecular,
pubmed-meshheading:10876244-Molecular Motor Proteins,
pubmed-meshheading:10876244-Molecular Sequence Data,
pubmed-meshheading:10876244-Molecular Weight,
pubmed-meshheading:10876244-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:10876244-Protein Binding,
pubmed-meshheading:10876244-Protein Structure, Secondary,
pubmed-meshheading:10876244-Ribonucleoprotein, U2 Small Nuclear,
pubmed-meshheading:10876244-Sequence Alignment,
pubmed-meshheading:10876244-Sequence Homology, Amino Acid,
pubmed-meshheading:10876244-Solutions,
pubmed-meshheading:10876244-Structure-Activity Relationship,
pubmed-meshheading:10876244-Surface Properties
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pubmed:year |
2000
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pubmed:articleTitle |
Solution structure of a dynein motor domain associated light chain.
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pubmed:affiliation |
Department of Biochemistry, University of Connecticut Health Center, 263 Farmington Avenue, Farmington, Connecticut 06032-3305, USA.
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pubmed:publicationType |
Journal Article
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