PDBsum entry 3w0i

Transcription

PDB id: 3w0i

Contents

Protein chains

242 a.a.

12 a.a.

Ligands

O11

Waters ×102

PDB id:

3w0i

Name:

Transcription

Title:

Crystal structure of rat vdr ligand binding domain in complex with novel nonsecosteroidal ligands

Structure:

Vitamin d3 receptor. Chain: a. Fragment: ligand binding domain, unp residues 121-159, 218-420. Synonym: vdr, 1,25-dihydroxyvitamin d3 receptor, nuclear receptor subfamily 1 group i member 1. Engineered: yes. Mediator of RNA polymerase ii transcription subunit 1. Chain: c. Fragment: drip 205 nr2 box peptide, unp residues 640-652.

Source:

Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: nr1i1, vdr. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Homo sapiens. Human.

Resolution:

1.90Å R-factor: 0.203 R-free: 0.279

Authors:

T.Shimizu,L.Asano,N.Kuwabara,I.Ito,T.Waku,J.Yanagisawa,H.Miyachi

Key ref:

L.Asano et al. (2013). Structural basis for vitamin D receptor agonism by novel non-secosteroidal ligands. Febs Lett, 587, 957-963. PubMed id: 23462137 DOI: 10.1016/j.febslet.2013.02.028

Date:

30-Oct-12 Release date: 09-Oct-13

Protein chain

P13053  (VDR_RAT) -  Vitamin D3 receptor from Rattus norvegicus

Seq: 423 a.a.

Struc: 242 a.a.

Protein chain

Q15648  (MED1_HUMAN) -  Mediator of RNA polymerase II transcription subunit 1 from Homo sapiens

Seq: 1581 a.a.

Struc: 12 a.a.

DOI no: 10.1016/j.febslet.2013.02.028

Febs Lett 587:957-963 (2013)

PubMed id: 23462137

Structural basis for vitamin D receptor agonism by novel non-secosteroidal ligands.

L.Asano, I.Ito, N.Kuwabara, T.Waku, J.Yanagisawa, H.Miyachi, T.Shimizu.

ABSTRACT

Non-secosteroidal ligands for vitamin D receptor (VDR) have been developed for the agonist with non-calcemic profiles. Here, we provide the structural mechanism of VDR agonism by novel non-secosteroidal ligands. All ligands had the similar efficacy, while two had the higher potency. Crystallographic analyses revealed that all ligands interacted with helix H10 and the loop between helices H6 and H7 in a similar manner, but also that the two ligands with higher potency had different interaction modes. This study suggests that distinct ligand potency depend upon differences in the formation and rearrangement of hydrogen-bond networks induced by each ligand.