CRYSTAL OF OXIDIZED LDL-RECOGNITION DOMAIN OF OXIDIZED LDL RECEPTOR LOX-1, STEREOSTRUCTURE THEREOF AND UTILIZATION OF THE SAME

摘要

In order to clarify the binding manner of an oxidized LDL receptor LOX-1 to oxidized LDL in detail, it is intended to clarify the stereostructure of the oxidized LDL-binding domain of LOX-1. In particular, it is finally intended to clarify the stereostructure of a CTLD-binding domain as a dimer structure holding the same pattern as occurring on the cell surface layer. The problem of clarifying the oxidized LDL-binding domain (CTLD: C-type lectin-like domain) of LOX-1 employed in crystallization and a protein containing the LOX-1 oxidized LDL-binding domain and an NECK domain (a region connecting a transmembrane part to the CTLD) occurring as a dimer can be solved by obtaining various crystals with the use of samples obtained by unwinding proteins expressed on a mass scale in Escherichia coli in accordance with the method disclosed in the description (preferably comprising the step of adding a buffer solution having a buffering region in the acidic pH range to a solution and the step of adding calcium or zinc ion to the solution, or the step of adding a buffer solution having a buffering region in the neutral pH range to the solution in the case of the LOX-1 dimer) and analyzing the thus obtained crystals.