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PDBsum entry 3e4u

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protein Protein-protein interface(s) links
Transcription PDB id
3e4u
Jmol
Contents
Protein chains
119 a.a. *
120 a.a. *
112 a.a. *
110 a.a. *
Waters ×256
* Residue conservation analysis
PDB id:
3e4u
Name: Transcription
Title: Crystal structure of the wild-type human bcl6 btb/poz domain
Structure: B-cell lymphoma 6 protein. Chain: a, b, c, d, e, f. Fragment: btb domain. Synonym: bcl-6, zinc finger protein 51, laz-3 protein, bcl- finger and btb domain-containing protein 27. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: bcl6, bcl5, laz3, zbtb27, znf51. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.10Å     R-factor:   0.221     R-free:   0.259
Authors: M.A.Stead,G.O.Rosbrook,J.M.Hadden,C.H.Trinh,S.B.Carr,S.C.Wri
Key ref: M.A.Stead et al. (2008). Structure of the wild-type human BCL6 POZ domain. Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 1101-1104. PubMed id: 19052359
Date:
12-Aug-08     Release date:   09-Dec-08    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P41182  (BCL6_HUMAN) -  B-cell lymphoma 6 protein
Seq:
Struc:
 
Seq:
Struc:
706 a.a.
119 a.a.
Protein chains
Pfam   ArchSchema ?
P41182  (BCL6_HUMAN) -  B-cell lymphoma 6 protein
Seq:
Struc:
 
Seq:
Struc:
706 a.a.
120 a.a.
Protein chain
Pfam   ArchSchema ?
P41182  (BCL6_HUMAN) -  B-cell lymphoma 6 protein
Seq:
Struc:
 
Seq:
Struc:
706 a.a.
112 a.a.
Protein chain
Pfam   ArchSchema ?
P41182  (BCL6_HUMAN) -  B-cell lymphoma 6 protein
Seq:
Struc:
 
Seq:
Struc:
706 a.a.
110 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 

 
Acta Crystallogr Sect F Struct Biol Cryst Commun 64:1101-1104 (2008)
PubMed id: 19052359  
 
 
Structure of the wild-type human BCL6 POZ domain.
M.A.Stead, G.O.Rosbrook, J.M.Hadden, C.H.Trinh, S.B.Carr, S.C.Wright.
 
  ABSTRACT  
 
BCL6 is a transcriptional repressor that is overexpressed in diffuse large B-cell lymphoma and follicular lymphoma. The N-terminal POZ domain of BCL6 interacts with transcriptional corepressors and targeting these associations is a promising therapeutic strategy. Previous structural studies of the BCL6 POZ domain have used a mutant form because of the low solubility of the wild-type recombinant protein. A method for the purification and crystallization of the wild-type BCL6 POZ domain is described and the crystal structure to 2.1 A resolution is reported. This will be relevant for the design of therapeutics that target BCL6 POZ-domain interaction interfaces.