STRUCTURE OF A DNA-BINDING PROTEIN INVOLVED IN THE IMMUNE RESPONSE

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。 T-bet是Th1T细胞分化的主要调节因子，对抗病毒免疫反应至关重要。我们从衍射率约为3.5°的晶体中获得了T-bet的DNA结合域的第一个粗略结构解决方案，它与共识结合序列的寡核苷酸形成了复合体。这一结构表明，与其他T-box结合蛋白相比，T-bet的相互作用模式有很大的不同。现在，我们有了一些不同条件下的晶体，我们希望这些晶体能显示出更好的衍射效果。此外，我们还生成了与各种不同的DNA寡聚体结合的蛋白质晶体。我们希望，这些额外的数据可以让我们为这种蛋白质产生一个更好的模型，并继续发表我们的发现。

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. T-bet is the master regulator of Th1 T-cell differentiation and is critical to anti-viral immune response. We produced the first rough structural solution of the DNA-binding domain of T-bet in complex with an oligonucleotide of the consensus binding sequence, from crystals that diffracted to about 3.5 ¿. The structure suggests a very interesting difference in the interaction mode of T-bet relative to other T-box binding proteins. Now, we have crystals from a number of different conditions that we hope will show improved diffraction. In addition, we have generated crystals of the protein bound to a variety of different DNA oligomers. We?re hopeful that this additional data could allow us to produce a much better model for this protein and proceed with publishing our findings.