CONTACT SITES BETWEEN RVDR AND VITAMIN D

这个子项目是利用由NIH/NCRR资助的中心拨款提供的资源的许多研究子项目之一。子项目和调查员(PI)可能从另一个NIH来源获得了主要资金，因此可能会出现在其他CRISE条目中。列出的机构是针对中心的，而不一定是针对调查员的机构。众所周知，色氨酸排列在VDR结合口袋内，并与环间5，7-二烯维生素部分平行定位。由于双键通常会屏蔽位于其下方的质子，我们预计色氨酸核的化学位移可能取决于维生素D双键的取向。两个色氨酸氮原子：主链和侧链与溶剂和邻近的氨基酸形成氢键。这些相互作用可以通过引起信号线加宽和改变化学位移来影响核磁共振谱。上述情况，再加上VDR中只存在一个Trp分子的事实，促使我们选择这种氨基酸作为确定维生素D-VDR复合体结合部位的方便探针。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. It is well established that tryptophan lines the VDR binding pocket and is positioned parallell to intercyclic 5,7-diene vitamin moieties. Since double bonds usually shield protons positioned under them, we expect that chemical shifts of tryptophan nuclei could be dependent on the orientation of vitamin D double bonds. Two tryptophan nitrogen atoms: backbone and side chain create hydrogen bonds with solvent and neighboring amino acids. These interactions can influence NMR spectra by causing signal line broadening and by changing chemical shifts. The above, combined with the fact that only one Trp molecule is present in VDR, motivated us to choose this amino acid as a convenient probe to determine binding sites in vitamin D-VDR complexes.