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鸡蛋壳丝蛋白 3 的 H、N 和 C 共振分配。

H, N and C resonance assignments of eggcase silk protein 3.

机构信息

School of Life Sciences, Tianjin University, Tianjin, 300072, P.R. China.

出版信息

Biomol NMR Assign. 2024 Dec;18(2):227-232. doi: 10.1007/s12104-024-10192-4. Epub 2024 Aug 24.

Abstract

Spider silk is a high-performance biomaterial known for its outstanding combination of strength and flexibility. Among the six distinct types of spider silk, eggcase silk stands out as it is exclusively produced from the tubuliform gland, playing a specialized role in offspring protection. In the spider species Latrodectus hesperus, eggcase silk is spun from a large spidroin complex, including the major silk component tubuliform spidroin 1 (TuSp1) and at least six different minor silk components. One of these minor components is eggcase protein 3 (ECP3), a small silk protein of 11.8 kDa that lacks the typical spidroin architecture. ECP3 shows very limited homology to all known spidroins. In this study, we report nearly complete backbone and side-chain resonance assignments of ECP3 as a basis for studying the structural mechanisms involved in eggcase silk formation.

摘要

蜘蛛丝是一种高性能的生物材料,以其出色的强度和柔韧性结合而闻名。在六种不同类型的蜘蛛丝中,卵袋丝尤为突出,因为它仅由管状腺产生,在保护后代方面发挥着特殊作用。在蜘蛛物种 Latrodectus hesperus 中,卵袋丝由一个大型丝蛋白复合物纺制而成,其中包括主要的丝成分管状丝蛋白 1(TuSp1)和至少六种不同的次要丝成分。这些次要成分之一是卵袋蛋白 3(ECP3),一种 11.8 kDa 的小丝蛋白,缺乏典型的丝蛋白结构。ECP3 与所有已知的丝蛋白显示出非常有限的同源性。在这项研究中,我们报告了 ECP3 的近完整的骨架和侧链共振分配,作为研究卵袋丝形成中涉及的结构机制的基础。

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