Pääkkönen Kimmo, Tossavainen Helena, Permi Perttu, Rakkolainen Harri, Rauvala Heikki, Raulo Erkki, Kilpeläinen Ilkka, Güntert Peter
Tatsuo Miyazawa Memorial Program, RIKEN Genomic Sciences Center, Yokohama, Japan.
Proteins. 2006 Aug 15;64(3):665-72. doi: 10.1002/prot.21030.
F-spondin is a protein mainly associated with neuronal development. It attaches to the extracellular matrix and acts in the axon guidance of the developing nervous system. F-spondin consists of eight domains, six of which are TSR domains. The TSR domain family binds a wide range of targets. Here we present the NMR solution structures of TSR1 and TSR4. TSR domains have an unusual fold that is characterized by a long, nonglobular shape, consisting of two beta-strands and one irregular extended strand. Three disulfide bridges and stack of alternating tryptophan and arginine side-chains stabilize the structure. TSR1 and TSR4 structures are similar to each other and to the previously determined TSR domain X-ray structures from another protein, TSP, although TSR4 exhibits a mobile loop not seen in other structures.
F-spondin是一种主要与神经元发育相关的蛋白质。它附着于细胞外基质，并在发育中的神经系统的轴突导向中发挥作用。F-spondin由八个结构域组成，其中六个是TSR结构域。TSR结构域家族能结合多种靶标。在此我们展示了TSR1和TSR4的核磁共振溶液结构。TSR结构域具有一种不寻常的折叠方式，其特点是呈长的、非球状形状，由两条β链和一条不规则的延伸链组成。三个二硫键以及交替排列的色氨酸和精氨酸侧链的堆叠稳定了该结构。TSR1和TSR4的结构彼此相似，且与先前从另一种蛋白质TSP确定的TSR结构域X射线结构相似，尽管TSR4呈现出一个在其他结构中未见的可移动环。
