Electron microscopic demonstration of a common structural motif in human complement factor C3 and rat α1 ‐inhibitor 3 (murinoglobulin)

FEBS Letters

Sinohara, Hyogo²  Saito, Akio¹  Arata, Yoji²  Nishigai, Masaaki³  Ikai, Atsushi³  Muto, Yutaka² 

[1] Department of Biochemistry, Kinki University, School of Medicine, Minamikawachi-gun Osaka, Japan;Faculty of Pharmaceutical Sciences, The University of Tokyo, Hongo, Tokyo, Japan;Laboratory of Biodynamics, Tokyo Institute of Technology, Nagatsuta, Midoriku, Yokohama, Japan

关键词: Complement factor C3;    α1-Inhibitor 3;    Electron micrograph;    Homologous protein structure;   

DOI  :  10.1016/0014-5793(90)80126-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Electron microscopy of two homologous giant proteins revealed that complement factor C3 and α_i-inhibitor 3 have a common structural motif of a semicircularly bent string 18–20 nm long with two or three bumps indicating globular domains. C3 had a structure similar to the letter C with a small but distinct hole in the center. α₁-Inhibitor 3 was a more complete ring sometimes ajar at one corner. When the latter was treated with a proteinase, it became slightly flattened and adopted a squarish C-shape.

【 授权许可】

Unknown