Parisi Gustavo, Fornasari María Silvina, Echave Julián
Universidad Nacional de Quilmes, Roque Sáenz Peña 180, B1876BXD Bernal, Argentina.
FEBS Lett. 2004 Mar 26;562(1-3):1-4. doi: 10.1016/S0014-5793(04)00165-6.
Dynactin is a multimeric protein essential for the minus-end-directed transport driven by microtubule-based motor dynein. The pointed-end subcomplex in dynactin contains p62, p27, p25, and Arp11 subunits, and is thought to participate in interactions with membranous cargoes. We used sequence and structure prediction analysis to study dynactins p25 and p27. Here we present evidence that strongly supports that dynactins p27 and p25 contain the isoleucine-patch motif and adopt the left-handed parallel beta-helix fold. The structural models we obtained could contribute to the understanding of the complex interactions that dynactins are able to establish with cargo particles, microtubules or other dynactin subunits.
动力蛋白激活蛋白是一种多聚体蛋白，对于由基于微管的动力蛋白驱动的负端定向运输至关重要。动力蛋白激活蛋白中的尖端部亚复合体包含p62、p27、p25和Arp11亚基，并被认为参与与膜性货物的相互作用。我们使用序列和结构预测分析来研究动力蛋白激活蛋白的p25和p27。在此，我们提供的证据有力地支持了动力蛋白激活蛋白的p27和p25含有异亮氨酸补丁基序并采用左手平行β-螺旋折叠。我们获得的结构模型有助于理解动力蛋白激活蛋白与货物颗粒、微管或其他动力蛋白激活蛋白亚基之间能够建立的复杂相互作用。
