4.5 Article

Structural investigation of the ligand binding domain of the zebrafish VDR in complexes with 1α,25(OH)2D3 and Gemini:: purification, crystallization and preliminary X-ray diffraction analysis

期刊

出版社

PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jsbmb.2004.03.109

关键词

VDR; LBD; crystal structure; 1 alpha,25(OH)(2)D-3; gemini; purification; crystallization

向作者/读者索取更多资源

The nuclear receptor of Vitamin D can be activated by a large number of agonist molecules with a wide spectrum in their stereochemical framework. Up to now most of our structural information related to the protein-ligand complex formation is based on an engineered ligand binding domain (LBD) of the human receptor. We now have extended our database, using a wild-type LBD from zebrafish that confirms the previously reported results and allows to investigate the binding of ligands that induce significant conformational changes at the protein level. (C) 2004 Elsevier Ltd. All rights reserved.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.5
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据