TY - JOUR AU - Wang, Wei AB -

Protein-protein interactions are essential for regulating almost all aspects of cellular functions. Many of these interactions are mediated by weak and transient protein domain-peptide binding, but they are often under-represented in high throughput screening of protein-protein interactions using techniques such as yeast two-hybrid and mass spectrometry. On the other hand, computational predictions and in vitro binding assays are valuable in providing clues of in vivo interactions. We present here a systematic approach that integrates computer modeling and a peptide microarray technology to identify binding peptides of the SH3 domain of the tyrosine kinase Abl1 in the human proteome. Our study provides a comprehensive list of candidate interacting partners for the Abl1 protein, among which the presence of numerous methyltransferases and RNA splicing proteins may suggest a novel function of Abl1 in chromatin remodeling and RNA processing. This study illustrates a powerful approach for integrating computational and experimental methods to detect protein interactions mediated by domain-peptide recognition.

TI - Proteome-wide Detection of Abl1 SH3-binding Peptides by Integrating Computational Prediction and Peptide Microarray * JF - Molecular & Cellular Proteomics DO - 10.1074/mcp.o111.010389 DA - 2012-01-01 UR - https://www.deepdyve.com/lp/american-society-for-biochemistry-and-molecular-biology/proteome-wide-detection-of-abl1-sh3-binding-peptides-by-integrating-WFse7EZwJ0 VL - 11 IS - 1 DP - DeepDyve ER -