Grewal N, Talwar G P, Salunke D M
National Institute of Immunology, New Delhi, India.
Protein Eng. 1994 Feb;7(2):205-11. doi: 10.1093/protein/7.2.205.
Primary structural homology between the hormone binding site of the LH/CG receptor and the enzyme binding site of chymotrypsin inhibitor has been identified. This has led to the application of a knowledge-based approach of molecular modelling to describe the interaction of choriogonadotropin (CG) with the LH/CG receptor. A tertiary structural model for the mode of recognition between the hormone and the receptor has been proposed. As in other such processes at the molecular level, the recognition between CG and its receptor is mediated through non-covalent interactions. The specificity of recognition is achieved by complementarity in van der Waals surfaces, hydrogen bonding and non-polar associations. The model shows nine hydrogen bonds between the hormone and the receptor involving polar side chains as well as backbone amine and carbonyl groups. A hydrophobic cluster involving side chain groups at the interface is also important in stabilization of the intermolecular interactions.
已确定促黄体生成素/绒毛膜促性腺激素（LH/CG）受体的激素结合位点与胰凝乳蛋白酶抑制剂的酶结合位点之间存在一级结构同源性。这促使人们应用基于知识的分子建模方法来描述绒毛膜促性腺激素（CG）与LH/CG受体的相互作用。已提出了一种关于激素与受体识别模式的三级结构模型。与分子水平上的其他此类过程一样，CG与其受体之间的识别是通过非共价相互作用介导的。识别的特异性是通过范德华表面的互补性、氢键和非极性缔合来实现的。该模型显示激素与受体之间有九个氢键，涉及极性侧链以及主链胺基和羰基。在界面处涉及侧链基团的疏水簇对分子间相互作用的稳定也很重要。
