School of Life Sciences, Tianjin University, Tianjin, 300072, People's Republic of China.
Tianjin Key Laboratory of Function and Application of Biological Macromolecular Structures, School of Life Sciences, Tianjin University, Tianjin, 300072, People's Republic of China.
Biomol NMR Assign. 2021 Oct;15(2):475-477. doi: 10.1007/s12104-021-10048-1. Epub 2021 Aug 26.
Spider silk is renowned for its excellent mechanical properties. Among six types of silk and one silk glue produced by different abdominal glands for various purposes, tubuliform (eggcase) silk is unique due to its high serine and low glycine content. Eggcase silk is spun from at least two spidroins, tubuliform spidroin 1 (TuSp1) and TuSp2. TuSp1 and TuSp2 were identified as the major and the minor components in tubuliform glands, respectively. TuSp2 consists of multiple repetitive (RP) domains with short terminal tails and shares very limited homology to all known spidroins. Here we report backbone and side chain resonance assignments of TuSp2-RP as a basis for structural and functional studies on eggcase silk formation.
蜘蛛丝以其优异的机械性能而闻名。在六种丝和一种丝胶中，不同的腹部腺体为不同的目的产生不同的丝和丝胶，而管状（卵壳）丝由于其高丝氨酸和低甘氨酸含量而独具特色。卵壳丝由至少两种丝蛋白纺制而成，即管状丝蛋白 1（TuSp1）和 TuSp2。TuSp1 和 TuSp2 分别被鉴定为管状腺中的主要和次要成分。TuSp2 由多个重复（RP）结构域和短的末端尾巴组成，与所有已知的丝蛋白共享非常有限的同源性。在这里，我们报道了 TuSp2-RP 的骨架和侧链共振分配，作为卵壳丝形成的结构和功能研究的基础。
