Merging extracellular domains: Fold prediction for laminin G-like and amino-terminal thrombospondin-like modules based on homology to pentraxins
Merging extracellular domains: Fold prediction for laminin G-like and amino-terminal thrombospondin-like modules based on homology to pentraxins
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DOI：
10.1006/jmbi.1997.1510
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发表时间：
1998-02-06
影响因子：
5.6
通讯作者：
Reich, JG
中科院分区：
文献类型：
--
作者：
Beckmann, G;Hanke, J;Reich, JG
使用序列共有串的构建和数据库搜索的新方法，我们鉴定了一个新的蛋白质模块超家族，包括层粘连蛋白 G、血小板反应蛋白 N 和五聚蛋白家族。保守模式主要对应于位于两种五聚蛋白、人C反应蛋白和血清淀粉样蛋白P组分的已知三维结构的中心β链中的疏水核心残基。因此，我们预测该超家族的所有成员都会出现类似的果冻卷折叠。此外，大多数超家族成员中两个暴露的天冬氨酸残基的保守性表明迄今为止尚未识别的功能位点。 (C) 1998 学术出版社有限公司。
Using a new method for construction and database searches of sequence consensus strings, we have identified a new superfamily of protein modules comprising laminin G, thrombospondin N and the pentraxin families. The conserved patterns correspond mainly to hydrophobic core residues located in central beta strands of the known three-dimensional structures of two pentraxins, the human C-reactive protein and the serum amyloid P-component. Thus, we predict a similar jellyroll fold for all members of this superfamily. Ln addition, the conservation of two exposed aspartate residues in the majority of superfamily members suggests hitherto unrecognised functional sites. (C) 1998 Academic Press Limited.