TRAF MOLECULES IN CELL SIGNALING

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 中心，不一定是研究者的机构。 肿瘤坏死因子受体是细胞信号传导中重要的细胞因子受体。 CD 40是该家族的一个充分表征的成员，其在B细胞上表达并触发免疫应答、免疫球蛋白类别转换和细胞凋亡的活化。 与CD 40一样，其它TNFR，如LT β受体和BAFF受体，以及来自Epstein巴尔病毒的癌蛋白LMP 1，与TRAF的胞质结构域结合以刺激细胞信号。 在一个连续的系列中，我们正在结晶TRAF 3与这些信号伴侣的功能片段的复合物。 为了研究结合的细节并确定信号传导的分子基础，将代表相互作用区域的合成肽浸入TRAF 3晶体中。 晶体通常不与标准的旋转阳极源的分辨率所需的详细的结合分析的水平。 因此，我们计划继续使用同步加速器X射线来收集复合物的数据。

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.