Heikkinen Outi, Permi Perttu, Koskela Harri, Ylänne Jari, Kilpeläinen Ilkka
Laboratory of Organic Chemistry, Department of Chemistry, University of Helsinki, A.I. Virtasen Aukio 1, P.O. Box 55, 00014, Helsinki, Finland.
Biomol NMR Assign. 2009 Jun;3(1):53-6. doi: 10.1007/s12104-008-9140-6. Epub 2009 Jan 4.
Filamins are large actin-binding and cross-linking proteins which act as linkers between the cytoskeleton and various signaling proteins. Filamin A (FLNa) is the most abundant of the three filamin isoforms found in humans. FLNa contains an N-terminal actin-binding domain and 24 immunoglobulin-like (Ig) domains. The Ig domains are responsible for the FLNa dimerization and most of the interactions that FLNa has with numerous other proteins. There are several crystal and solution structures from isolated single Ig domains of filamins in the PDB database, but only few from longer constructs. Here, we present nearly complete chemical shift assignments of FLNa tandem Ig domains 16-17 and 18-19. Chemical shift mapping between FLNa tandem Ig domain 16-17 and isolated domain 17 suggests a novel domain-domain interaction mode.
细丝蛋白是一类大型的肌动蛋白结合和交联蛋白，作为细胞骨架与各种信号蛋白之间的连接物发挥作用。细丝蛋白A（FLNa）是人类中发现的三种细丝蛋白异构体中含量最丰富的一种。FLNa包含一个N端肌动蛋白结合结构域和24个免疫球蛋白样（Ig）结构域。Ig结构域负责FLNa的二聚化以及FLNa与众多其他蛋白质的大部分相互作用。蛋白质数据银行（PDB）数据库中有来自细丝蛋白单个分离Ig结构域的多个晶体结构和溶液结构，但来自更长构建体的结构很少。在此，我们给出了FLNa串联Ig结构域16 - 17和18 - 19几乎完整的化学位移归属。FLNa串联Ig结构域16 - 17与分离的结构域17之间的化学位移图谱表明了一种新的结构域 - 结构域相互作用模式。
