CRYSTAL STRUCTURES OF ARP2/3 COMPLEX WITH BOUND NUCLEOTIDE AND ACTIVATOR

该子项目是利用NIH/NCRR资助的中心赠款提供的资源的许多研究子项目之一。子项目和研究者（PI）可能从另一个NIH来源获得主要资金，因此可以在其他CRISP条目中表示。所列机构为中心，不一定是研究者所在机构。Arp 2/3复合物是一个223 kD的7个蛋白质的组装体，它使肌动蛋白丝的生长成核。这一过程发生在运动细胞的主要激发期，被认为在细胞运动中起重要作用。Arp 2/3复合物本质上是无活性的，并且需要可水解的ATP、预先存在的肌动蛋白丝和一种或多种活化蛋白质以使丝成核。我们的目标是在分子水平上了解这种复合物的功能。先前已经解决了非活性复合物的晶体结构，我们目前正在研究具有结合激活剂和核苷酸的复合物的结构，以了解复合物是如何被激活的。

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. Arp2/3 complex is an 223kD assembly of seven proteins that nucleates the growth of actin filaments. This process occurs at the leading enge of motile cells and is thought to play an important role in cell motility. Arp2/3 complex is intrinisically inactive and requires hydrolysable ATP, pre-existing actin fiilament, and one or more activating proteins in order to nucleate filaments. We aim to understand the function of this complex at the molecular level. The crystal structure of the inactive coplex has been previously solved, and we are currently working on structures of the complex with bound activators and nucleotides to get an idea of how the complex is activated.