Inwardly rectifying, voltage-gated, two-pore domain, and related K+ channels are located in eukaryotic membranes rich in cholesterol. Here, molecular docking is used to detect specific binding sites ("hot spots") for cholesterol on K+ channels with characteristics that match those of known cholesterol binding sites. The transmembrane surfaces of all available high-resolution structures for K+ channels were swept for potential binding sites. Cholesterol poses were found to be located largely in hollows between protein ridges. A comparison between cholesterol poses and resolved phospholipids suggests that not all cholesterol molecules binding to the transmembrane surface of a K+ channel will result in displacement of a phospholipid molecule from the surface. Competition between cholesterol binding and binding of anionic phospholipids essential for activity could explain some of the effects of cholesterol on channel function.

中文翻译：

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Kir、Kv、K2P 和相关钾通道上胆固醇的界面结合位点

内向整流、电压门控、双孔结构域和相关 K+ 通道位于富含胆固醇的真核细胞膜中。此处，分子对接用于检测 K+ 通道上胆固醇的特异性结合位点（“热点”），其特征与已知胆固醇结合位点的特征相匹配。扫描所有可用的 K+ 通道高分辨率结构的跨膜表面以寻找潜在的结合位点。发现胆固醇位姿主要位于蛋白质脊之间的空洞中。胆固醇形态和解析磷脂之间的比较表明，并非所有与 K+ 通道跨膜表面结合的胆固醇分子都会导致磷脂分子从表面移位。胆固醇结合和活性所必需的阴离子磷脂结合之间的竞争可以解释胆固醇对通道功能的一些影响。