3-DIMENSIONAL STRUCTURE OF A TRANSGLUTAMINASE - HUMAN BLOOD-COAGULATION FACTOR-XIII
3-DIMENSIONAL STRUCTURE OF A TRANSGLUTAMINASE - HUMAN BLOOD-COAGULATION FACTOR-XIII
复制标题
DOI：
10.1073/pnas.91.15.7296
复制
发表时间：
1994-07-19
影响因子：
11.1
通讯作者：
TELLER, DC
中科院分区：
文献类型：
--
作者：
YEE, VC;PEDERSEN, LC;TELLER, DC
许多生物材料中的机械稳定性是通过γ-谷氨酰-ε-赖氨酰酰胺键交联大结构蛋白质来提供的。人重组因子XIII的三维结构（EC 2.3.2.13 zymogen;蛋白质-谷氨酰胺：胺γ-谷氨酰转移酶α链），一种转氨酶酶原，已经通过X射线晶体学以2.8埃分辨率解析。该结构显示同源二聚体蛋白质的每条链折叠成四个连续的结构域。在核心结构域中已经鉴定出一个催化三联体，这让人想起在半胱氨酸蛋白酶中观察到的催化三联体。每个亚基的氨基末端活化肽穿过晚餐界面并部分封闭第二提交中的催化腔的开口，防止底物与酶原结合。凝血酶和钙激活机制的建议，详细说明了导致活性因子XIIIa '的结构事件。
Mechanical stability in many biological materials is provided by the crosslinking of large structural proteins with gamma-glutamyl-epsilon-lysyl amide bonds. The three-dimensional structure of human recombinant factor XIII (EC 2.3.2.13 zymogen; protein-glutamine:amine gamma-glutamyltransferase a chain), a transglutaminase zymogen, has been solved at 2.8-Angstrom resolution by x-ray crystallography. This structure shows that each chain of the homodimeric protein is folded into four sequential domains. A catalytic triad reminiscent of that observed in cysteine proteases has been identified in the core domain. The amino-terminal activation peptide of each subunit crosses the diner interface and partially occludes the opening of the catalytic cavity in the second submit, preventing substrate binding to the zymogen. A proposal for the mechanism of activation by thrombin and calcium is made that details the structural events leading to active factor XIIIa'.