Dissociation and subunit rearrangement of membrane-bound human C-reactive proteins.
As one of the most important acute-phase reactants in human serum, C-reactive protein plays its physiological roles mainly on membranes. Here we show that the human C-reactive protein is two-dimensionally crystallized upon specific adsorption on the phosphorylcholine ligand containing membranes by monolayer approach. The 2.0-nm resolution projection structure of the two-dimensional crystals analyzed by electron microscopy and image reconstruction reveals open-ring-like pentamers in the crystals. The electron microscope graphs also show that the dissociated pentamers with open-ring-like structure occur in a closed packing region (not two-dimensionally crystallized). These results indicate a membrane-induced dissociation and rearrangement of hCRP, which may relate to the variety of hCRP's physiological functions.
Wang
H W
HW
Department of Biological Sciences and Biotechnology, State Key Laboratory of Biomembranes, Tsinghua University, Beijing 100084, China.
Sui
S F
SF
D002097:C-Reactive Protein / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D003460:Crystallization; D006801:Humans; D008081:Liposomes / Q000378:metabolism; D008244:Lysophosphatidylcholines / Q000378:metabolism; D010063:Ovum / Q000737:chemistry; D010767:Phosphorylcholine / Q000378:metabolism; D021122:Protein Subunits
D008081:Liposomes; D008244:Lysophosphatidylcholines; D021122:Protein Subunits; D010767:Phosphorylcholine; D002097:C-Reactive Protein