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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2000-5-9
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pubmed:databankReference |
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pubmed:abstractText |
Rab geranylgeranyltransferase (RabGGT) catalyzes the addition of two geranylgeranyl groups to the C-terminal cysteine residues of Rab proteins, which is crucial for membrane association and function of these proteins in intracellular vesicular trafficking. Unlike protein farnesyltransferase (FT) and type I geranylgeranyltransferase, which both prenylate monomeric small G proteins or short peptides, RabGGT can prenylate Rab only when Rab is in a complex with Rab escort protein (REP).
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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 |
Mar
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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 |
241-51
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:10745007-Alkyl and Aryl Transferases,
pubmed-meshheading:10745007-Amino Acid Sequence,
pubmed-meshheading:10745007-Animals,
pubmed-meshheading:10745007-Binding Sites,
pubmed-meshheading:10745007-Crystallography, X-Ray,
pubmed-meshheading:10745007-Models, Molecular,
pubmed-meshheading:10745007-Molecular Sequence Data,
pubmed-meshheading:10745007-Peptides,
pubmed-meshheading:10745007-Protein Conformation,
pubmed-meshheading:10745007-Protein Prenylation,
pubmed-meshheading:10745007-Rats,
pubmed-meshheading:10745007-Sequence Homology, Amino Acid,
pubmed-meshheading:10745007-Zinc
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pubmed:year |
2000
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pubmed:articleTitle |
Crystal structure of Rab geranylgeranyltransferase at 2.0 A resolution.
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pubmed:affiliation |
Department of Biochemistry, Howard Hughes Medical Institute, The University of Texas Southwestern Medical Center, Dallas, 75235-9050, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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