Imai N, Masugi F, Ogihara T, Kumahara Y, Hirose S, Akiyama F, Murakami K
Biochem Biophys Res Commun. 1984 Sep 17;123(2):452-7. doi: 10.1016/0006-291x(84)90251-1.
The nature of the hormone-binding site of detergent-solubilized angiotensin II receptor from the bovine adrenal cortex has been characterized using diaminoalkanes. Their affinity for the hormone-binding site showed a dramatic alteration depending on their chain length; at the hexamethylene stage, a maximum and competitive inhibition was observed. These results indicate that the angiotensin II receptors have a definite hydrophobic binding groove limbed with diagonally located two negative charges, and those hydrophobic and electrostatic forces may play an important role in the proper register between the receptor and hormone.
利用二氨基烷烃对来自牛肾上腺皮质的去污剂增溶血管紧张素II受体的激素结合位点的性质进行了表征。它们对激素结合位点的亲和力根据链长显示出显著变化；在己烷阶段，观察到最大和竞争性抑制。这些结果表明，血管紧张素II受体具有一个明确的疏水结合凹槽，两侧对角排列着两个负电荷，并且这些疏水和静电力可能在受体与激素之间的正确配准中起重要作用。
