SAXS OF A PROTEIN COMPLEX FORMED BY VGCC B4C AND CHROMO SHADOW DOMAIN OF HP1

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 VGCC b4c与HP1染色影结构域形成的蛋白质复合体的小角X射线散射 电压门控钙通道(VGCC)β4亚基的短剪接形式与核蛋白异染色质蛋白1(HP1)相互作用，调节基因沉默。兽医比尔·霍恩博士和S博士在体外通过下拉实验、ITC和核磁共振波谱证实了截短的VGCC b4与HP1的染色影结构域(CSD)之间形成了复合体。Horne博士(Pi)和他的博士后徐兴福博士想要用小角X射线散射来确定这种复合体的分子包膜，并验证从核磁共振对接得到的结构模型。

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. Small-angle X-ray Scattering of a protein complex formed by VGCC b4c and chromo shadow domain of HP1 A short splicing form of voltage-gated chalcium channel (VGCC) beta 4 subunit interacts with a nuclear protein Heterochromotin Protein 1 (HP1) and regulates gene silencing. The complex formation between the truncated VGCC b4 and chromo shadow domain (CSD) of HP1 has been confirmed in vitro by pull down experiment, ITC and NMR spectroscopy in Dr. Bill Horne¿¿"s group in Vet school. Dr. Horne (PI) and his postdoc Dr. Xingfu Xu want to determine the molecular envelope of this complex using Small-angle X-ray scattering and validate the structure model derived from NMR docking.