Crystal structure of human coactosin-like protein at 1.9 A resolution.
Human coactosin-like protein (CLP) shares high homology with coactosin, a filamentous (F)-actin binding protein, and interacts with 5LO and F-actin. As a tumor antigen, CLP is overexpressed in tumor tissue cells or cell lines, and the encoded epitopes can be recognized by cellular and humoral immune systems. To gain a better understanding of its various functions and interactions with related proteins, the crystal structure of CLP expressed in Escherichia coli has been determined to 1.9 A resolution. The structure features a central beta-sheet surrounded by helices, with two very tight hydrophobic cores on each side of the sheet. CLP belongs to the actin depolymerizing protein superfamily, and is similar to yeast cofilin and actophilin. Based on our structural analysis, we observed that CLP forms a polymer along the crystallographic b axis with the exact same repeat distance as F-actin. A model for the CLP polymer and F-actin binding has therefore been proposed.
Li
Xuemei
X
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, People's Republic of China.
Liu
Xueqi
X
Lou
Zhiyong
Z
Duan
Xin
X
Wu
Hao
H
Liu
Yiwei
Y
Rao
Zihe
Z
D000199:Actins / Q000737:chemistry; D000951:Antigens, Neoplasm / Q000737:chemistry; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D006801:Humans; D008840:Microfilament Proteins / Q000737:chemistry*; D008958:Models, Molecular; D011485:Protein Binding; D017433:Protein Structure, Secondary
D000199:Actins; D000951:Antigens, Neoplasm; C118115:COTL1 protein, human; D008840:Microfilament Proteins