Crystal structure of human lectin-like, oxidized low-density lipoprotein receptor 1 ligand binding domain and its ligand recognition mode to OxLDL |
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Authors: | Ohki Izuru Ishigaki Tomoko Oyama Takuji Matsunaga Shigeru Xie Qiuhong Ohnishi-Kameyama Mayumi Murata Takashi Tsuchiya Daisuke Machida Sachiko Morikawa Kousuke Tate Shin-ichi |
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Affiliation: | Department of Structural Biology, Biomolecular Engineering Research Institute 6-2-3, Furuedai, Suita, Osaka, 565-0874, Japan. |
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Abstract: | Lectin-like, oxidized low-density lipoprotein (LDL) receptor 1, LOX-1, is the major receptor for oxidized LDL (OxLDL) in endothelial cells. We have determined the crystal structure of the ligand binding domain of LOX-1, with a short stalk region connecting the domain to the membrane-spanning region, as a homodimer linked by an interchain disulfide bond. In vivo assays with LOX-1 mutants revealed that the "basic spine," consisting of linearly aligned arginine residues spanning over the dimer surface, is responsible for ligand binding. Single amino acid substitution in the dimer interface caused a severe reduction in LOX-1 binding activity, suggesting that the correct dimer arrangement is crucial for binding to OxLDL. Based on the LDL model structure, possible binding modes of LOX-1 to OxLDL are proposed. |
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