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PDBsum entry 3tx7

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protein ligands Protein-protein interface(s) links
Protein binding PDB id
3tx7

 

 

 

 

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Contents
Protein chains
504 a.a.
218 a.a.
Ligands
P6L
PDB id:
3tx7
Name: Protein binding
Title: Crystal structure of lrh-1/beta-catenin complex
Structure: Catenin beta-1. Chain: a. Synonym: beta-catenin. Engineered: yes. Nuclear receptor subfamily 5 group a member 2. Chain: b. Synonym: alpha-1-fetoprotein transcription factor, b1-binding factor, hb1f, cyp7a promoter-binding factor, hepatocytic transcription factor, liver receptor homolog 1, lrh-1.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ctnnb1, ctnnb, ok/sw-cl.35, pro2286. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: nr5a2, b1f, cpf, ftf.
Resolution:
2.76Å     R-factor:   0.201     R-free:   0.243
Authors: F.Yumoto,R.Fletterick
Key ref: F.Yumoto et al. (2012). Structural basis of coactivation of liver receptor homolog-1 by β-catenin. Proc Natl Acad Sci U S A, 109, 143-148. PubMed id: 22187462
Date:
22-Sep-11     Release date:   14-Dec-11    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P35222  (CTNB1_HUMAN) -  Catenin beta-1 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
781 a.a.
504 a.a.
Protein chain
Pfam   ArchSchema ?
O00482  (NR5A2_HUMAN) -  Nuclear receptor subfamily 5 group A member 2 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
541 a.a.
218 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
Proc Natl Acad Sci U S A 109:143-148 (2012)
PubMed id: 22187462  
 
 
Structural basis of coactivation of liver receptor homolog-1 by β-catenin.
F.Yumoto, P.Nguyen, E.P.Sablin, J.D.Baxter, P.Webb, R.J.Fletterick.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
22504882 P.M.Musille, M.C.Pathak, J.L.Lauer, W.H.Hudson, P.R.Griffin, and E.A.Ortlund (2012).
Antidiabetic phospholipid-nuclear receptor complex reveals the mechanism for phospholipid-driven gene regulation.
  Nat Struct Mol Biol, 19, 532.
PDB codes: 4dor 4dos
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. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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