NDLI: Three-dimensional modeling of and ligand docking to vitamin D receptor ligand binding domain

Content Provider	PubMed Central
Author	Yamamoto, Keiko Masuno, Hiroyuki Choi, Mihwa Nakashima, Kinichi Taga, Tetsuya Hiroshi, Ooizumi Umesono, Kazuhiko Wanda, Sicinska Vanhooke, Janeen Deluca, Hector F. Yamada, Sachiko
Copyright Year	2000
Abstract	The ligand binding domain of the human vitamin D receptor (VDR) was modeled based on the crystal structure of the retinoic acid receptor. The ligand binding pocket of our VDR model is spacious at the helix 11 site and confined at the β-turn site. The ligand 1α,25-dihydroxyvitamin D3 was assumed to be anchored in the ligand binding pocket with its side chain heading to helix 11 (site 2) and the A-ring toward the β-turn (site 1). Three residues forming hydrogen bonds with the functionally important 1α- and 25-hydroxyl groups of 1α,25-dihydroxyvitamin D3 were identified and confirmed by mutational analysis: the 1α-hydroxyl group is forming pincer-type hydrogen bonds with S237 and R274 and the 25-hydroxyl group is interacting with H397. Docking potential for various ligands to the VDR model was examined, and the results are in good agreement with our previous three-dimensional structure-function theory.
Related Links	http://dx.doi.org/10.1073/pnas.020522697
Ending Page	1472
Page Count	6
Starting Page	1467
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	4
Volume Number	97
Language	English
Publisher	The National Academy of Sciences
Publisher Date	2000-02-15
Access Restriction	Open
Rights Holder	The National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Three-dimensional modeling of and ligand docking to vitamin D receptor ligand binding domain.

Relationship between Structure and Conformational Change of the Vitamin D Receptor Ligand Binding Domain in 1α,25-Dihydroxyvitamin D3 Signaling

Identification of an alternative ligand-binding pocket in the nuclear vitamin D receptor and its functional importance in 1α,25(OH)2-vitamin D3 signaling

LIGAND INDEPENDENT ACTIONS OF VITAMIN D RECEPTOR

Three-dimensional structural model of the serine receptor ligand-binding domain.

The molecular structure of the Toll-like receptor 3 ligand-binding domain

Crystal structures of complexes of vitamin D receptor ligand-binding domain with lithocholic acid derivatives

Large-scale expression and purification of the human vitamin D receptor and its ligand-binding domain for structural studies.

Energetics of glutamate receptor ligand binding domain dimer assembly are modulated by allosteric ions

Three-dimensional modeling of and ligand docking to vitamin D receptor ligand binding domain

Similar Documents

Three-dimensional modeling of and ligand docking to vitamin D receptor ligand binding domain.

Relationship between Structure and Conformational Change of the Vitamin D Receptor Ligand Binding Domain in 1α,25-Dihydroxyvitamin D3 Signaling

Identification of an alternative ligand-binding pocket in the nuclear vitamin D receptor and its functional importance in 1α,25(OH)2-vitamin D3 signaling

LIGAND INDEPENDENT ACTIONS OF VITAMIN D RECEPTOR

Three-dimensional structural model of the serine receptor ligand-binding domain.

The molecular structure of the Toll-like receptor 3 ligand-binding domain

Crystal structures of complexes of vitamin D receptor ligand-binding domain with lithocholic acid derivatives

Large-scale expression and purification of the human vitamin D receptor and its ligand-binding domain for structural studies.

Energetics of glutamate receptor ligand binding domain dimer assembly are modulated by allosteric ions

Three-dimensional modeling of and ligand docking to vitamin D receptor ligand binding domain