|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
2
|
|
pubmed:dateCreated |
2000-3-9
|
|
pubmed:abstractText |
The protein farnesyltransferase (FTase) catalyzes addition of the hydrophobic farnesyl isoprenoid to a cysteine residue fourth from the C terminus of several protein acceptors that are essential for cellular signal transduction such as Ras and Rho. This addition is necessary for the biological function of the modified proteins. The majority of Ras-related human cancers are associated with oncogenic variants of K-RasB, which is the highest affinity natural substrate of FTase. Inhibition of FTase causes regression of Ras-mediated tumors in animal models.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Feb
|
|
pubmed:issn |
0969-2126
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
15
|
|
pubmed:volume |
8
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
209-22
|
|
pubmed:dateRevised |
2010-3-24
|
|
pubmed:meshHeading |
pubmed-meshheading:10673434-Alkyl and Aryl Transferases,
pubmed-meshheading:10673434-Amino Acid Sequence,
pubmed-meshheading:10673434-Animals,
pubmed-meshheading:10673434-Crystallography, X-Ray,
pubmed-meshheading:10673434-Enzyme Inhibitors,
pubmed-meshheading:10673434-Magnesium,
pubmed-meshheading:10673434-Molecular Mimicry,
pubmed-meshheading:10673434-Oncogene Protein p21(ras),
pubmed-meshheading:10673434-Protein Binding,
pubmed-meshheading:10673434-Protein Conformation,
pubmed-meshheading:10673434-Rats,
pubmed-meshheading:10673434-Substrate Specificity,
pubmed-meshheading:10673434-Zinc
|
|
pubmed:year |
2000
|
|
pubmed:articleTitle |
The basis for K-Ras4B binding specificity to protein farnesyltransferase revealed by 2 A resolution ternary complex structures.
|
|
pubmed:affiliation |
Department of Biochemistry, PO Box 3711, Duke University Medical Center, Durham, 27710, USA.
|
|
pubmed:publicationType |
Journal Article
|
