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

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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).