Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2003-10-6
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1097-2765
pubmed:author
pubmed:issnType
Print
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
615-25
pubmed:dateRevised
2005-11-21
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
pubmed:year
2003
pubmed:articleTitle
Conserved structural motifs in intracellular trafficking pathways: structure of the gammaCOP appendage domain.
pubmed:affiliation
Department of Molecular Medicine, Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.
pubmed:publicationType
Journal Article