Back to Search
Start Over
Selection of v-Abl Tyrosine Kinase Substrate Sequences from Randomized Peptide and Cellular Proteomic Libraries Using mRNA Display
- Source :
- Chemistry & Biology. (2):253-264
- Publisher :
- Cell Press. Published by Elsevier Ltd.
-
Abstract
- Methodologies for rapidly identifying cellular protein interactions resulting in posttranslational modification of one of the partners are lacking. Here, we select for substrates of the v-abl tyrosine kinase from two protein display libraries in which the protein is covalently linked to its encoding mRNA. Successive selection cycles from a randomized peptide library identified a consensus sequence closely matching that previously reported for the v-abl tyrosine kinase. Selections from a proteomic library derived from cellular mRNA identified several novel targets of v-abl, including a new member of a class of SH2 domain-containing adaptor proteins. Upon modification, several of the substrates obtained in these selections were found to be effective inhibitors of v-abl kinase activity in vitro. These experiments establish a novel method for identifying the substrates of tyrosine kinases from synthetic and cellular protein libraries.
- Subjects :
- Recombinant Fusion Proteins
Molecular Sequence Data
Clinical Biochemistry
Bone Marrow Cells
Protein tyrosine phosphatase
Biology
SH2 domain
Biochemistry
SH3 domain
Receptor tyrosine kinase
Substrate Specificity
Peptide Library
Drug Discovery
Humans
mRNA display
Amino Acid Sequence
RNA, Messenger
Phosphorylation
Kinase activity
Oncogene Proteins v-abl
Molecular Biology
Pharmacology
General Medicine
Protein-Tyrosine Kinases
Molecular biology
ROR1
biology.protein
Molecular Medicine
Proto-oncogene tyrosine-protein kinase Src
Subjects
Details
- Language :
- English
- ISSN :
- 10745521
- Issue :
- 2
- Database :
- OpenAIRE
- Journal :
- Chemistry & Biology
- Accession number :
- edsair.doi.dedup.....6979d3eef26fa739440d24c1cd898574
- Full Text :
- https://doi.org/10.1016/S1074-5521(02)00098-4