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人类C1r和C1s的结构及其与其他丝氨酸蛋白酶的关系。

The structures of human C1r and C1s and their relationship to other serine proteases.

作者信息

Fothergill J, Kemp G, Paton N, Carter P, Gray P

机构信息

Department of Biochemistry, University of Aberdeen, Marischal College, U.K.

出版信息

Behring Inst Mitt. 1989 Jul(84):72-9.

PMID:2552983
Abstract

The recent sequencing of the C1 subcomponents has allowed comparison with other molecules of homologous primary structure. Where tertiary structures are available for at least one member of the family it is possible to make further progress by modelling the amino acid sequence of the complement protein into the three-dimensional coordinates of the directly determined structure, thereby obtaining an approximation of the structure of the complement protein. Molecular modelling allows structure-function relationships to be explored and suggests further experiments that may be amenable to techniques such as site-directed mutagenesis.

摘要

最近对C1亚成分进行的测序使得能够与具有同源一级结构的其他分子进行比较。如果该家族中至少有一个成员的三级结构已知,那么通过将补体蛋白的氨基酸序列模拟到直接测定结构的三维坐标中,就有可能取得进一步进展,从而获得补体蛋白结构的近似值。分子模拟有助于探索结构与功能的关系,并为诸如定点诱变等技术可能适用的进一步实验提供思路。

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