PDBsum entry 2pog

Lipid binding protein

PDB id

2pog

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Contents

			Protein chains

					233 a.a. *


					211 a.a. *

			Ligands

					WST ×2

			Waters ×118

* Residue conservation analysis

PDB id:

2pog

Links

Name:

Lipid binding protein

Title:

Benzopyrans as selective estrogen receptor b agonists (serbas). Part 2: structure activity relationship studies on the benzopyran scaffold.

Structure:

Estrogen receptor. Chain: a, b. Fragment: ligand binding domain (residues 304-551). Synonym: er, estradiol receptor, er-alpha. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: esr1. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.84Å

R-factor:

0.235

R-free:

0.252

Authors:

T.I.Richardson,B.H.Norman,C.W.Lugar,S.A.Jones,Y.Wang,J.D.Durbin, V.Krishnan,J.A.Dodge

Key ref:

T.I.Richardson et al. (2007). Benzopyrans as selective estrogen receptor beta agonists (SERBAs). Part 2: structure-activity relationship studies on the benzopyran scaffold. Bioorg Med Chem Lett, 17, 3570-3574. PubMed id: 17485205 DOI: 10.1016/j.bmcl.2007.04.051

Date:

26-Apr-07

Release date:

11-Sep-07

PROCHECK

	Headers

	References

Protein chain

P03372 (ESR1_HUMAN) - Estrogen receptor from Homo sapiens

Seq: Struc:

Seq: Struc:					595 a.a. 233 a.a.*

Protein chain

P03372 (ESR1_HUMAN) - Estrogen receptor from Homo sapiens

Seq: Struc:

Seq: Struc:					595 a.a. 211 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 4 residue positions (black crosses)



		Enzyme reactions

Enzyme class:

Chains A, B: E.C.?

[IntEnz] [ExPASy] [KEGG] [BRENDA]

DOI no: 10.1016/j.bmcl.2007.04.051	Bioorg Med Chem Lett 17:3570-3574 (2007)
PubMed id: 17485205

Benzopyrans as selective estrogen receptor beta agonists (SERBAs). Part 2: structure-activity relationship studies on the benzopyran scaffold.
T.I.Richardson, B.H.Norman, C.W.Lugar, S.A.Jones, Y.Wang, J.D.Durbin, V.Krishnan, J.A.Dodge.

ABSTRACT

Benzopyrans are selective estrogen receptor (ER) beta agonists (SERBAs), which bind the ER subtypes alpha and beta in opposite orientations. Here we describe structure-activity relationship studies that led to the discovery of bezopyran 5b. X-ray crystal structures of 5b and a non-selective analog 5c in ERalpha help explain the observed selectivity of the benzopyran platform.

Literature references that cite this PDB file's key reference

PubMed id

Reference

19967775

F.Minutolo, M.Macchia, B.S.Katzenellenbogen, and J.A.Katzenellenbogen (2011).
Estrogen receptor β ligands: recent advances and biomedical applications.

Med Res Rev, 31, 364-442.

19293997

J.P.Salisbury, and J.C.Williams (2009).
Docking study of triphenylphosphonium cations as estrogen receptor alpha modulators.

Bioinformation, 3, 303-307.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.