121st General Meeting of the KCS

Type Poster Presentation
Area Physical Chemistry
Room No. Event Hall
Time 4월 20일 (금요일) 11:00~12:30
Code PHYS.P-141
Subject Cryogenic ion spectroscopy of DYYVVR to locate the phosphorylation site of Janus kinase 3
Authors MIN JI LEE, Jang Han Kwon, Hyuk Kang1,*
Department of Energy Systems Research, Ajou University, Korea
1Department of Chemistry, Ajou University, Korea
Abstract Protein phosphorylation is a considerably important post-translational modification, which usually occurs in an OH functional group of tyrosine, serine and methionine in the protein. Above all, phosphorylation of tyrosine does a significant role as signal transduction in a cell. Several researches have been conducted to find how such phosphorylation happens. For example, a research that uses antibody PY20, which perceives tyrosine in the protein, can tell if this amino acid is phosphorylated or not through SDS PAGE and western blotting. These methods are comparatively easy ways to find the phosphorylated tyrosine, however, is not suitable for investigating which tyrosine is the phosphorylation site in the protein. Thus, our goal is to investigate which tyrosine sites are involved in the phosphorylation by means of cryogenic ion spectroscopy. One of the tyrosine kinases, Janus kinase 3 (abbreviated as ‘JAK3’) has Y980 and Y981 (980th and 981st tyrosine residues), where Y980 positively regulates its kinase activity and Y981 negatively regulates itself. These JAK3’s Y980 and Y981 are a fine model for protein phosphorylation research, thus a hexapeptide DYYVVR (JAK3979-984) that is expected to be obtained by dealing JAK3 with trypsin is prepared. Our ultimate goal is to investigate tyrosine phosphorylation sites by comparing DYYVVR and phosphorylated ones (DpYYVVR, DYpYVVR, and DpYpYVVR). Before the final goal, a preparatory stage may be an identification of the difference between two tyrosines in DYYVVR. We conducted a UV photodissociation spectroscopy on DYYVVR, DFYVVR (Y980F), and DYFVVR (Y981F) to identify respective UV absorption peak of two tyrosines. Also, we assigned conformers of DYYVVR by hole burning spectroscopy.
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