2HVC

The Crystal Structure of Ligand-binding Domain (LBD) of human Androgen Receptor in Complex with a selective modulator LGD2226


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.253 
  • R-Value Work: 0.221 
  • R-Value Observed: 0.251 

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Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history


Literature

Structure of the ligand-binding domain (LBD) of human androgen receptor in complex with a selective modulator LGD2226

Wang, F.Liu, X.-Q.Li, H.Liang, K.-N.Miner, J.N.Hong, M.Kallel, E.A.van Oeveren, A.Zhi, L.Jiang, T.

(2006) Acta Crystallogr Sect F Struct Biol Cryst Commun 62: 1067-1071

  • DOI: https://doi.org/10.1107/S1744309106039340
  • Primary Citation of Related Structures:  
    2HVC

  • PubMed Abstract: 

    The androgen receptor (AR) is a ligand-inducible steroid hormone receptor that mediates androgen action, determining male sexual phenotypes and promoting spermatogenesis. As the androgens play a dominant role in male sexual development and function, steroidal androgen agonists have been used clinically for some years. However, there is a risk of potential side effects and most steroidal androgens cannot be dosed orally, which limits the use of these substances. 1,2-Dihydro-6-N,N-bis(2,2,2-trifluoroethyl)amino-4-trifluoromethyl-2-quinolinone (LGD2226) is a synthetic nonsteroidal ligand and a novel selective AR modulator. The crystal structure of the complex of LGD2226 with the androgen receptor ligand-binding domain (AR LBD) at 2.1 A was solved and compared with the structure of the AR LBD-R1881 complex. It is hoped that this will aid in further explaining the selectivity of LGD2226 observed in in vitro and in vivo assays and in developing more selective and effective therapeutic agents.


  • Organizational Affiliation

    National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing 100101, People's Republic of China.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Androgen receptor250Homo sapiensMutation(s): 0 
Gene Names: ARDHTRNR3C4
UniProt & NIH Common Fund Data Resources
Find proteins for P10275 (Homo sapiens)
Explore P10275 
Go to UniProtKB:  P10275
PHAROS:  P10275
GTEx:  ENSG00000169083 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP10275
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
LGD
Query on LGD

Download Ideal Coordinates CCD File 
B [auth A]6-[BIS(2,2,2-TRIFLUOROETHYL)AMINO]-4-(TRIFLUOROMETHYL)QUINOLIN-2(1H)-ONE
C14 H9 F9 N2 O
ULBPQWIGZUGPHU-UHFFFAOYSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
LGD BindingDB:  2HVC Ki: min: 1.5, max: 4.6 (nM) from 2 assay(s)
EC50: 0.2 (nM) from 1 assay(s)
PDBBind:  2HVC Ki: 1.5 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.253 
  • R-Value Work: 0.221 
  • R-Value Observed: 0.251 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 57.64α = 90
b = 65.39β = 90
c = 72.17γ = 90
Software Package:
Software NamePurpose
MOLREPphasing
CNSrefinement
d*TREKdata reduction
CrystalCleardata scaling

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2007-07-31
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2023-10-25
    Changes: Data collection, Database references, Derived calculations, Refinement description