Huang F Y, Yang Q X, Huang T H, Gelbaum L, Kuyper L F
School of Physics, Georgia Institute of Technology, Atlanta 30332.
FEBS Lett. 1991 May 20;283(1):44-6. doi: 10.1016/0014-5793(91)80549-i.
We have employed 15N and 31P NMR techniques to characterize the conformations of trimethoprim (TMP)/E. coli dihydrofolate reductase (DHFR) complexes in the presence and absence of NADPH and NADP+. A single conformation was observed for TMP/DHFR, NADP+/DHFR, NADPH/DHFR, and TMP/NADPH/DHFR complexes. In the ternary complex of TMP/NADP+/DHFR both the 15N and 31P spectra revealed the presence of two conformations. However, the conformations of TMP and NADP+ in the ternary complex may not be correlated, resulting in the possible existence of four conformations for the protein ternary complex.
我们运用了¹⁵N和³¹P核磁共振技术来表征甲氧苄啶（TMP）/大肠杆菌二氢叶酸还原酶（DHFR）复合物在存在和不存在烟酰胺腺嘌呤二核苷酸磷酸（NADPH）及烟酰胺腺嘌呤二核苷酸磷酸（NADP⁺）情况下的构象。对于TMP/DHFR、NADP⁺/DHFR、NADPH/DHFR和TMP/NADPH/DHFR复合物，观察到单一构象。在TMP/NADP⁺/DHFR三元复合物中，¹⁵N和³¹P光谱均显示存在两种构象。然而，三元复合物中TMP和NADP⁺的构象可能不相关，这导致蛋白质三元复合物可能存在四种构象。
