家蚕铁蛋白与少棘蜈蚣铁蛋白样分子变体的结构功能分析及比较

用生物信息学方法分析了家蚕的一个铁蛋白(gi 95102694)的结构与功能。结果显示该分子具有典型的4螺旋束结构,保留了亚铁氧化酶中心的全部功能部位,由此推测其为家蚕的功能铁蛋白H亚基。将其与从少棘蜈蚣(Scolopendra subspinipes mutilans)毒腺中获得的一个铁蛋白样变体比较,发现后者不仅因终止突变使C端被截短,也因多处错义突变丧失了保守的功能残基,由此推测其为少棘蜈蚣毒腺中表达的一个假基因产物。对产生该假基因产物的可能原因进行了讨论。分析结果有助于进一步研究家蚕铁蛋白的结构功能及其功能应用。

Analysis and comparison on structure and function of a ferritin from Bombyx mori and a ferritin-like variant from Scolopendra subspinipes mutilans

Structure and function of a ferritin from Bombyx mori(gi 95102694)was analyzed by bioinformatics method.Results showed it took the typical 4-bundle helical structure and containing whole conserved motifs for ferroxidase center,so it was suggested to be a ferritin H subunit of Bombyx mori.The BmFTH was further compared to a ferritin-like variant from venom gland of Scolopendra subspinipes mutilans.The later was found not only be shortened at C-term caused by a stop mutation,but also lost its functional residues by lot of missense mutations,so it was considered as a pseudogene of ferrin expressed in the tissue.Possible mechanisms of pseudogene expression in the centipede venom gland were discussed.Results presented here will provide favorable reference for further research on the relationship between structure and function of ferritin of silkworm and its application.