Molecular Modeling, Affinity Labeling, and Site-Directed Mutagenesis Define the Key Points of Interaction between the Ligand-Binding Domain of the Vitamin D Nuclear Receptor and 1α,25-Dihydroxyvitamin D3-Reference-Cited by-同舟云学术

Molecular Modeling, Affinity Labeling, and Site-Directed Mutagenesis Define the Key Points of Interaction between the Ligand-Binding Domain of the Vitamin D Nuclear Receptor and 1α,25-Dihydroxyvitamin D3

Published:2000-09-08 Issue:40 Volume:39 Page:12162-12171
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Swamy Narasimha¹,Xu Wenrong¹,Paz Nancy¹,Hsieh Jui-Cheng¹,Haussler Mark R.¹,Maalouf George J.¹,Mohr Scott C.¹,Ray Rahul¹

Affiliation:

1. Bioorganic Chemistry and Structural Biology Group, Vitamin D Laboratory, Department of Medicine, Boston University School of Medicine, Boston, Massachusetts 02118, Department of Chemistry, Boston University, Boston, Massachusetts 02215, Department of Biochemistry, University of Arizona, College of Medicine, Tucson, Arizona 85724, and Computational Biology, Compaq Computer Corporation, 200 Forest Street, Marlboro, Massachusetts 01752

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi0002131

Reference63 articles.

1. The Nuclear Vitamin D Receptor: Biological and Molecular Regulatory Properties Revealed

2. Current Understanding of the Molecular Actions of Vitamin D

3. Receptors for 1α,25(OH)2D3: Past, Present, and Future

4. Evolution of the nuclear receptor gene superfamily.

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