| pubmed-article:1992464 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1992464 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
| pubmed-article:1992464 | lifeskim:mentions | umls-concept:C1882598 | lld:lifeskim |
| pubmed-article:1992464 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:1992464 | lifeskim:mentions | umls-concept:C1519249 | lld:lifeskim |
| pubmed-article:1992464 | lifeskim:mentions | umls-concept:C0138837 | lld:lifeskim |
| pubmed-article:1992464 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:1992464 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:1992464 | pubmed:dateCreated | 1991-3-8 | lld:pubmed |
| pubmed-article:1992464 | pubmed:abstractText | We tested 42 tetrapeptides for their ability to bind to the rat brain p21ras protein farnesyltransferase as estimated by their ability to compete with p21Ha-ras in a farnesyltransfer assay. Peptides with the highest affinity had the structure Cys-A1-A2-X, where positions A1 and A2 are occupied by aliphatic amino acids and position X is occupied by a COOH-terminal methionine, serine, or phenylalanine. Charged residues reduced affinity slightly at the A1 position and much more drastically at the A2 and X positions. Effective inhibitors included tetrapeptides corresponding to the COOH termini of all animal cell proteins known to be farnesylated. In contrast, the tetrapeptide Cys-Ala-Ile-Leu (CAIL), which corresponds to the COOH termini of several neural guanine nucleotide binding (G) protein gamma subunits, did not compete in the farnesyl-transfer assay. Inasmuch as several of these proteins are geranylgeranylated, the data suggest that the two isoprenes (farnesyl and geranylgeranyl) are transferred by different enzymes. A biotinylated heptapeptide corresponding to the COOH terminus of p21Ki-rasB was farnesylated, suggesting that at least some of the peptides serve as substrates for the transferase. The data are consistent with a model in which a hydrophobic pocket in the protein farnesyltransferase recognizes tetrapeptides through interactions with the cysteine and the last two amino acids. | lld:pubmed |
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| pubmed-article:1992464 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1992464 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1992464 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1992464 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1992464 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:1992464 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:1992464 | pubmed:author | pubmed-author:BrownM SMS | lld:pubmed |
| pubmed-article:1992464 | pubmed:author | pubmed-author:GoldsteinJ... | lld:pubmed |
| pubmed-article:1992464 | pubmed:author | pubmed-author:GieraschL MLM | lld:pubmed |
| pubmed-article:1992464 | pubmed:author | pubmed-author:StradleyS JSJ | lld:pubmed |
| pubmed-article:1992464 | pubmed:author | pubmed-author:ReissYY | lld:pubmed |
| pubmed-article:1992464 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1992464 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:1992464 | pubmed:volume | 88 | lld:pubmed |
| pubmed-article:1992464 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1992464 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1992464 | pubmed:pagination | 732-6 | lld:pubmed |
| pubmed-article:1992464 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:1992464 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1992464 | pubmed:articleTitle | Sequence requirement for peptide recognition by rat brain p21ras protein farnesyltransferase. | lld:pubmed |
| pubmed-article:1992464 | pubmed:affiliation | Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas 75235. | lld:pubmed |
| pubmed-article:1992464 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1992464 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1992464 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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