PHOSPHORYLATED TAMNDEM SH2 DOMAINS OF PHOSPHOLIPASE C GAMMA 1

这个子项目是利用由NIH/NCRR资助的中心拨款提供的资源的许多研究子项目之一。子项目和调查员(PI)可能从另一个NIH来源获得了主要资金，因此可能会出现在其他CRISE条目中。列出的机构是针对中心的，而不一定是针对调查员的机构。PLCg的SH2结构域在酪氨酸783(Y783)被磷酸化后发生分子内结构的变化，该结构位于C端SH2结构域的C末端延伸处。Y783的磷酸化导致磷酸化的Y783(PY783)与C-末端SH2结构域之间的分子内相互作用，导致PLCg的激活(Poulin等，PNAS，2005)。我构建了两个串联的SH2结构域，C端延伸，含有PLCg的Y783，并表达、纯化和磷酸化Y783，用大分子X射线结晶学在原子水平上阐明PLCg的激活。我得到了有希望的磷酸化PLCg片段的初始蛋白质晶体。

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.