Format

Send to

Choose Destination
Genome Biol. 2005;6(6):R55. Epub 2005 May 27.

Refinement and prediction of protein prenylation motifs.

Author information

1
IMP - Research Institute of Molecular Pathology, Dr, Bohr-Gasse 7, A-1030 Vienna, Austria. stroh@imp.univie.ac.at

Abstract

We refined the motifs for carboxy-terminal protein prenylation by analysis of known substrates for farnesyltransferase (FT), geranylgeranyltransferase I (GGT1) and geranylgeranyltransferase II (GGT2). In addition to the CaaX box for the first two enzymes, we identify a preceding linker region that appears constrained in physicochemical properties, requiring small or flexible, preferably hydrophilic, amino acids. Predictors were constructed on the basis of sequence and physical property profiles, including interpositional correlations, and are available as the Prenylation Prediction Suite (PrePS, http://mendel.imp.univie.ac.at/sat/PrePS) which also allows evaluation of evolutionary motif conservation. PrePS can predict partially overlapping substrate specificities, which is of medical importance in the case of understanding cellular action of FT inhibitors as anticancer and anti-parasite agents.

PMID:
15960807
PMCID:
PMC1175975
DOI:
10.1186/gb-2005-6-6-r55
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for BioMed Central Icon for PubMed Central
Loading ...
Support Center