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rdf:type |
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lifeskim:mentions |
umls-concept:C0003732,
umls-concept:C0018296,
umls-concept:C0026336,
umls-concept:C0439849,
umls-concept:C0444626,
umls-concept:C0445223,
umls-concept:C0678594,
umls-concept:C0995925,
umls-concept:C1420408,
umls-concept:C1523873,
umls-concept:C1552599,
umls-concept:C1704787,
umls-concept:C1705535,
umls-concept:C1707455
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pubmed:issue |
5
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pubmed:dateCreated |
2000-7-13
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pubmed:abstractText |
Protein targeting to the endoplasmic reticulum in eukaryotes and to the cell membrane in prokaryotes is mediated by the signal recognition particle (SRP) and its receptor (SR). Both contain conserved GTPase domains in the signal-peptide-binding proteins (SRP54 and Ffh) and the SR proteins (SRalpha and FtsY). These GTPases are involved in the regulation of protein targeting. Most studies so far have focussed on the SRP machinery of mammals and bacteria, leaving the SRP system of archaea less well understood.
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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 |
0969-2126
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
515-25
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10801496-Archaea,
pubmed-meshheading:10801496-Bacterial Proteins,
pubmed-meshheading:10801496-Binding Sites,
pubmed-meshheading:10801496-Conserved Sequence,
pubmed-meshheading:10801496-Crystallography, X-Ray,
pubmed-meshheading:10801496-Escherichia coli Proteins,
pubmed-meshheading:10801496-GTP Phosphohydrolases,
pubmed-meshheading:10801496-Models, Molecular,
pubmed-meshheading:10801496-Molecular Sequence Data,
pubmed-meshheading:10801496-Nucleotides,
pubmed-meshheading:10801496-Protein Binding,
pubmed-meshheading:10801496-Protein Structure, Tertiary,
pubmed-meshheading:10801496-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:10801496-Sequence Homology, Amino Acid,
pubmed-meshheading:10801496-Signal Recognition Particle,
pubmed-meshheading:10801496-Signal Transduction
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pubmed:year |
2000
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pubmed:articleTitle |
The crystal structure of the conserved GTPase of SRP54 from the archaeon Acidianus ambivalens and its comparison with related structures suggests a model for the SRP-SRP receptor complex.
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pubmed:affiliation |
European Molecular Biology Laboratory, Structural Biology Programme, Heidelberg, D-69017, Germany.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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