Screening of Peptide Libraries to Investigate the Substrate Specificity of UL97 Protein Kinase from Human Cytomegalovirus.
10.4167/jbv.2006.36.2.119
- Author:
Moon Chang BAEK
1
Author Information
1. Department of Molecular Medicine, School of Medicine, Kyungpook National University, Daegu, Korea. mcbaek@knu.ac.kr
- Publication Type:Original Article
- Keywords:
Human cytomegalovirus;
Protein kinase UL97;
Peptide substrate;
Peptide library
- MeSH:
Amino Acids;
Cytomegalovirus*;
Ganciclovir;
Histones;
Humans*;
Mass Screening*;
Peptide Library*;
Peptides;
Phosphorylation;
Protein Kinases*;
Substrate Specificity*
- From:Journal of Bacteriology and Virology
2006;36(2):119-124
- CountryRepublic of Korea
- Language:Korean
-
Abstract:
Human cytomegalovirus encodes an unusual protein kinase UL97 which can phosphorylate exogenous substrates, including histone H2B and nucleoside analogs such as ganciclovir. The previous result interestingly showed that the peptides phosphorylated by UL97 have K/R at the 5 positions (P+5) downstream from the pSer. To confirm the importance of the basic residue in the position, we used two peptide libraries, 4S4K (MAXXXXSXXXXKXANNN) and 4S6N (MAXXXXSXXXXXXNNN). The activity of phosphorylation by UL97 was higher in the peptide library 4S4K than 4S6N, suggesting the importance of basic residue at P+5 position. The screening with a peptide library 4S4K showed slight tendencies for N in the P+1 and P+2, M in the P+2, K in the P+4 and P+6 positions and several amino acids in the other positions. This result will give information to develop an optimal peptide for screening a novel UL97 inhibitor.
