Section of Cell Biology and Biophysics, Department of Biology, School of Sciences, National and Kapodistrian University of Athens, Panepistimiopolis, Athens 157 01, Greece.
Section of Cell Biology and Biophysics, Department of Biology, School of Sciences, National and Kapodistrian University of Athens, Panepistimiopolis, Athens 157 01, Greece.
J Mol Biol. 2018 Oct 12;430(20):3774-3783. doi: 10.1016/j.jmb.2018.06.042. Epub 2018 Jun 28.
Silkmoth chorion is a fibrous structure composed mainly of two major protein classes, families A and B. Both families of silkmoth chorion proteins present a highly conserved, in sequence and in length, central domain, consisting of Gly-rich tandem hexapeptide repetitive segments, flanked by two more variable N-terminal and C-terminal arms. Primary studies identified silkmoth chorion as a functional protective amyloid by unveiling the amyloidogenic properties of the central domain of both protein families. In this work, we attempt to detect the principal source of amyloidogenicity of the central domain by focusing on the role of the tandem hexapeptide sequence repeats. Concurrently, we discuss a possible mechanism for the self-assembly of class A protofilaments, suggesting that the aggregation-prone hexapeptide building blocks may fold into a triangle-shaped β-helical structure.
家蚕卵壳是一种纤维结构，主要由两类主要蛋白质家族 A 和 B 组成。家蚕卵壳蛋白的这两个家族都具有高度保守的序列和长度，中央结构域由富含甘氨酸的串联六肽重复片段组成，两端是两个更可变的 N 端和 C 端臂。初步研究表明，卵壳蛋白具有功能保护的淀粉样特性，揭示了两个蛋白家族中央结构域的淀粉样特性，从而将其鉴定为功能性保护性淀粉样蛋白。在这项工作中，我们试图通过关注串联六肽序列重复的作用来检测中央结构域的主要淀粉样形成性来源。同时，我们讨论了 A 类原纤维自组装的可能机制，表明倾向于聚集的六肽构建块可能折叠成三角形 β-螺旋结构。
