TRAF MOLECULES IN CELL SIGNALING

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。 肿瘤坏死因子受体是在细胞信号转导中起重要作用的细胞因子受体。CD40是该家族中的一员，表达于B细胞上，可触发免疫反应、免疫球蛋白类别转换和激活细胞凋亡。和CD40一样，其他TNFR，如LTβ受体和BAFF受体，以及Epstein Barr病毒的癌蛋白LMP1，都与TRAF的细胞质结构域相关，以刺激细胞信号。在一个连续的系列中，我们正在结晶与每个信号伙伴的功能片段结合在一起的TRAF3。为了研究结合的细节并确定信号的分子基础，代表相互作用区域的合成肽被浸泡到TRAF3晶体中。晶体通常不会用标准的旋转阳极源衍射到详细结合分析所需的分辨率水平。因此，我们计划继续使用同步加速器x射线来收集复合体的数据。

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. Tumor necrosis factor receptors are cytokine receptors important in cellular signaling. CD40 is a well-characterized member of this family that is expressed on B cells and triggers immune responses, immunoglobulin class switching and activation of apoptosis. Like CD40, other TNFRs, such as LTbeta receptor and BAFF receptor, as well as the oncoprotein LMP1 from Epstein Barr Virus, associate with the cytoplasmic domain of TRAFs to stimulate cell signals. In a continuing series, we are crystallizing TRAF3 bound in complex with the functional fragments of each of these signaling partners. To study the details of binding and define the molecular basis for signaling, synthetic peptides representing the interacting regions are soaked into TRAF3 crystals. The crystals do not typically diffract with a standard rotating anode source to the level of resolution required for detailed binding analyses. Therefore we plan to continue using synchrotron x-rays to collect data for the complexes.