CRYSTALS OF THE DYNEIN MICROTUBULE BINDING DOMAIN FUSED TO SERYL-TRNA SYNTHETASE

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。 动力蛋白通过末端有6个螺旋结构域的反平行长卷绕结合到微管上。ATP与动力蛋白头部的结合很可能沿着卷曲的线圈传递到微管结合结构域(MTBD)，从结构角度来看，这可能是非常有趣的。我们已经将MTBD和部分茎融合到丝氨酰-tRNA合成酶上的卷曲线圈上。我的合作者已经证明，通过改变融合部位，我们可以调节MTBD对微管的亲和力。我们现在有了这些结构之一的晶体(弱结合形式)。

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. Dynein binds to microtubules via a long antiparallel coiled coil with a 6 helix domain at the tip. Binding of ATP to the head of the dynein is likely to be communicated to the microtubule binding domain (MTBD) along the coiled coil and how this occurs is likely to be very interesting from a structural perspective. We have fused the MTBD and part of the stalk to the coiled coil found on seryl-tRNA synthetase. My collaborator has shown that be varying the site of fusion we can modulate the affinity of the MTBD for microtubules. We now have crystals of one of these constructs (the weak binding form).