Source:http://linkedlifedata.com/resource/pubmed/id/14527408
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2003-10-6
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pubmed:databankReference | |
pubmed:abstractText |
The formation of coated vesicles is a fundamental step in many intracellular trafficking pathways. COPI and clathrin represent two important and distinct sets of vesicle coating machinery, involved primarily in mediating intra-Golgi and endocytic transport, respectively. Here we identify an important functional region at the carboxyl terminus of the gamma subunit of the COPI complex (gammaCOP) and describe the X-ray crystal structure of this domain at 2.3 A resolution. This domain of gammaCOP exhibits unexpected structural similarity to the carboxyl-terminal appendage domains of the alpha and beta subunits of the AP2 adaptor proteins, integral components of clathrin-coated vesicles. The remarkable structural conservation exhibited by the gammaCOP appendage domain, coupled with functional data and primary sequence analysis, supports a model of COPI function with significant structural and mechanistic parallels to vesicular transport by the clathrin/AP2 system.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1097-2765
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pubmed:author | |
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 |
615-25
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pubmed:dateRevised |
2005-11-21
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pubmed:meshHeading |
pubmed-meshheading:14527408-Adaptor Protein Complex 2,
pubmed-meshheading:14527408-Amino Acid Motifs,
pubmed-meshheading:14527408-Carrier Proteins,
pubmed-meshheading:14527408-Coated Vesicles,
pubmed-meshheading:14527408-Coatomer Protein,
pubmed-meshheading:14527408-Conserved Sequence,
pubmed-meshheading:14527408-Eukaryotic Cells,
pubmed-meshheading:14527408-Evolution, Molecular,
pubmed-meshheading:14527408-Intracellular Fluid,
pubmed-meshheading:14527408-Models, Molecular,
pubmed-meshheading:14527408-Molecular Sequence Data,
pubmed-meshheading:14527408-Molecular Structure,
pubmed-meshheading:14527408-Phylogeny,
pubmed-meshheading:14527408-Protein Structure, Tertiary,
pubmed-meshheading:14527408-Protein Transport,
pubmed-meshheading:14527408-Saccharomyces cerevisiae,
pubmed-meshheading:14527408-Sequence Homology, Amino Acid,
pubmed-meshheading:14527408-Sequence Homology, Nucleic Acid
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pubmed:year |
2003
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pubmed:articleTitle |
Conserved structural motifs in intracellular trafficking pathways: structure of the gammaCOP appendage domain.
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pubmed:affiliation |
Department of Molecular Medicine, Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.
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pubmed:publicationType |
Journal Article
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