PHOSPHORYLATED TAMNDEM SH2 DOMAINS OF PHOSPHOLIPASE C GAMMA 1

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The intramolecular structure of SH2 domains of PLCg changes upon phosphorylation of Tyrosine 783 (Y783), which is located at the C-terminal extension of C-terminal SH2 domain. The phosphorylation of Y783 causes the intramolecular interaction between phosphorylated Y783 (pY783) and C-terminal SH2 domain resulting in the activation of PLCg (Poulin, et al, PNAS, 2005). I made a construct of 2 tandem SH2 domains with a C-terminal extension containing Y783 of PLCg and expressed, purified and phosphorylated Y783 to elucidate the activation of PLCg in atomic level using macromolecular X-ray crystallography. I obtained promising initial protein crystals of phosphorylated PLCg fragment.