U.O.S. Biopolimeri e Proteomica. IRCCS A.O.U. San Martino - IST, Istituto Nazionale per la Ricerca sul Cancro, Largo R. Benzi 10, 16132 Genova Italy.
Curr Med Chem. 2012;19(36):6199-206.
G-Protein Coupled Receptor (GPCR) superfamily, which comprises approximately 900 members, is the largest family of protein targets with proven therapeutic value. Although at least 500 GPCRs have been identified as therapeutically relevant, only thirteen GPCRs have been structurally characterized in apo-form or in complex with ligands. GPCRs share relatively low sequence similarity making hard the process of homology modelling, nevertheless some successful hits have been determined. Recently, the G-protein-coupled estrogen receptor 1 (GPER, formerly known as GPR30) has attracted increasing interest due to its ability in mediating estrogen signaling in different normal and cancer tissues. In this regard, the identification of selective GPER ligands has provided valuable tools in order to differentiate the specific functions elicited by this novel estrogen receptor respect to those exerted by the classical estrogen receptors (ERs). In this review, we focus on GPER examining "in silico" docking simulations and evaluating the different binding modes of diverse natural and synthetic ligands.
G 蛋白偶联受体（GPCR）超家族是最大的蛋白质靶标家族之一，包含约 900 个成员，具有已证实的治疗价值。尽管已经确定了至少 500 个 GPCR 具有治疗相关性，但仅有 13 个 GPCR 以apo 形式或与配体复合物的形式在结构上得到了表征。GPCR 具有相对较低的序列相似性，使得同源建模过程变得困难，但已经确定了一些成功的命中。最近，由于其在不同正常和癌症组织中介导雌激素信号的能力，G 蛋白偶联雌激素受体 1（GPER，以前称为 GPR30）引起了越来越多的关注。在这方面，选择性 GPER 配体的鉴定为区分该新型雌激素受体与经典雌激素受体（ERs）所发挥的特定功能提供了有价值的工具。在这篇综述中，我们重点介绍了 GPER，研究了“计算”对接模拟，并评估了不同天然和合成配体的不同结合模式。
