人补体丝氨酸蛋白酶C1r和C1s及其酶原。 - Suppr | 超能文献

Human complement serine proteases C1r and C1s and their proenzymes.

作者信息

Arlaud G J, Thielens N M

机构信息

Institut de Biologie Structurale, Laboratoire d'Enzymologie Moléculaire, Grenoble, France.

出版信息

Methods Enzymol. 1993;223:61-82. doi: 10.1016/0076-6879(93)23038-o.

DOI:10.1016/0076-6879(93)23038-o

Abstract

摘要

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Complement C1q Interacts With LRP1 Clusters II and IV Through a Site Close but Different From the Binding Site of Its C1r and C1s-Associated Proteases.补体 C1q 通过一个接近但不同于其 C1r 和 C1s 相关蛋白酶结合位点的位点与 LRP1 簇 II 和 IV 相互作用。

Front Immunol. 2020 Oct 21;11:583754. doi: 10.3389/fimmu.2020.583754. eCollection 2020.

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Mapping surface accessibility of the C1r/C1s tetramer by chemical modification and mass spectrometry provides new insights into assembly of the human C1 complex.通过化学修饰和质谱法绘制 C1r/C1s 四聚体的表面可及性图谱，为研究人 C1 复合物的组装提供了新的见解。

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Calcium-dependent conformational flexibility of a CUB domain controls activation of the complement serine protease C1r.钙离子依赖的 CUB 结构域构象灵活性控制补体丝氨酸蛋白酶 C1r 的激活。

J Biol Chem. 2010 Apr 16;285(16):11863-9. doi: 10.1074/jbc.M109.098541. Epub 2010 Feb 23.

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Crystal structure of the catalytic domain of human complement c1s: a serine protease with a handle.人补体C1s催化结构域的晶体结构：一种带有柄的丝氨酸蛋白酶。

EMBO J. 2000 Apr 17;19(8):1755-65. doi: 10.1093/emboj/19.8.1755.