形成纽结：斯帕茨勒蛋白的结构与激活模型
Getting knotted: a model for the structure and activation of Spätzle.
作者信息
Mizuguchi K, Parker J S, Blundell T L, Gay N J
机构信息
Dept of Biochemistry, University of Cambridge, UK.
出版信息
Trends Biochem Sci. 1998 Jul;23(7):239-42. doi: 10.1016/s0968-0004(98)01216-x.
PMID:9697410
Abstract
Sequence analyses show that Spätzle, the Drosophila melanogaster Toll-receptor ligand, shows striking similarity to nerve growth factor and coagulogen. Comparative modelling suggests that Spätzle adopts a cystine-knot fold and forms a dimer that contains a single, intermolecular disulphide bridge. Proteolytically cleaved Spätzle could therefore dimerize and activate the Toll receptor by inducing receptor dimerization.
摘要
序列分析表明，果蝇Toll受体配体斯帕兹勒（Spätzle）与神经生长因子和凝聚原具有显著的相似性。比较建模表明，斯帕兹勒采用胱氨酸结折叠并形成一个二聚体，该二聚体包含一个分子间二硫键。因此，经蛋白水解切割的斯帕兹勒可以通过诱导受体二聚化而二聚化并激活Toll受体。
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