PHOSPHORYLATED TAMNDEM SH2 DOMAINS OF PHOSPHOLIPASE C GAMMA 1

本子项目是利用由NIH/NCRR资助的中心赠款提供的资源的众多研究子项目之一。子项目和研究者（PI）可能已经从另一个NIH来源获得了主要资金，因此可以在其他CRISP条目中表示。列出的机构是中心的，不一定是研究者的机构。PLCg SH2结构域的分子内结构在酪氨酸783 （Y783）磷酸化后发生变化，酪氨酸783位于c端SH2结构域的c端延伸。Y783的磷酸化导致磷酸化的Y783 （pY783）与c端SH2结构域之间的分子内相互作用导致PLCg的激活（Poulin等，PNAS, 2005）。我构建了含有PLCg的Y783的2个串联SH2结构域的c端延伸，并表达、纯化和磷酸化了Y783，利用大分子x射线晶体学在原子水平上阐明了PLCg的活化。我获得了磷酸化PLCg片段的有希望的初始蛋白质晶体。

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.