Bernard P, Guedin D, Hibert M
Laboratoire de Pharmacochimie de la Communication Cellulaire, UMR CNRS/ULP 7081, Faculté de Pharmacie, 74 route du Rhin, 67400 Illkirch-Graffenstaden, France.
J Med Chem. 2001 Jan 4;44(1):27-35. doi: 10.1021/jm000915o.
A three-dimensional model of the extracellular domain of the GABA(B) receptor has been built by homology with the leucine/isoleucine/valine-binding protein. The complete putative GABA-binding site in the extracellular domain is described in both the open and closed states. The dynamics of the "Venus flytrap" mechanism has been studied, suggesting that the molecular dipole moments play a key role in GABA binding and receptor activation. Important residues putatively implicated either in ligand binding or in the dynamics of the receptor are pinpointed, thus highlighting target residues for mutagenesis experiments and model validation.
通过与亮氨酸/异亮氨酸/缬氨酸结合蛋白同源建模，构建了GABA(B)受体细胞外结构域的三维模型。描述了细胞外结构域中处于开放和关闭状态的完整假定GABA结合位点。研究了“捕蝇草”机制的动力学，表明分子偶极矩在GABA结合和受体激活中起关键作用。确定了可能与配体结合或受体动力学有关的重要残基，从而突出了用于诱变实验和模型验证的目标残基。
