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PDBsum entry 2ly4

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protein Protein-protein interface(s) links
Nuclear protein/antitumour protein PDB id
2ly4
Jmol
Contents
Protein chains
83 a.a.
47 a.a.
PDB id:
2ly4
Name: Nuclear protein/antitumour protein
Title: Hmgb1-facilitated p53 DNA binding occurs via hmg-box/p53 transactivation domain interaction and is regulated by the tail
Structure: High mobility group protein b1. Chain: a. Synonym: high mobility group protein 1, hmg-1. Engineered: yes. Cellular tumor antigen p53. Chain: b. Synonym: antigen ny-co-13, phosphoprotein p53, tumor suppre engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hmg1, hmgb1. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: p53, tp53.
NMR struc: 10 models
Authors: J.P.Rowell,K.L.Simpson,K.Stott,M.Watson,J.O.Thomas
Key ref: J.P.Rowell et al. (2012). HMGB1-facilitated p53 DNA binding occurs via HMG-Box/p53 transactivation domain interaction, regulated by the acidic tail. Structure, 20, 2014-2024. PubMed id: 23063560 DOI: 10.1016/j.str.2012.09.004
Date:
12-Sep-12     Release date:   31-Oct-12    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P09429  (HMGB1_HUMAN) -  High mobility group protein B1
Seq:
Struc:
215 a.a.
83 a.a.
Protein chain
Pfam   ArchSchema ?
P04637  (P53_HUMAN) -  Cellular tumor antigen p53
Seq:
Struc:
393 a.a.
47 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     nucleus   1 term 
  Biological process     apoptotic process   2 terms 
  Biochemical function     DNA binding     2 terms  

 

 
DOI no: 10.1016/j.str.2012.09.004 Structure 20:2014-2024 (2012)
PubMed id: 23063560  
 
 
HMGB1-facilitated p53 DNA binding occurs via HMG-Box/p53 transactivation domain interaction, regulated by the acidic tail.
J.P.Rowell, K.L.Simpson, K.Stott, M.Watson, J.O.Thomas.
 
  ABSTRACT  
 
Facilitated binding of p53 to DNA by high mobility group B1 (HMGB1) may involve interaction between the N-terminal region of p53 and the high mobility group (HMG) boxes, as well as HMG-induced bending of the DNA. Intramolecular shielding of the boxes by the HMGB1 acidic tail results in an unstable complex with p53 until the tail is truncated to half its length, at which point the A box, proposed to be the preferred binding site for p53(1-93), is exposed, leaving the B box to bind and bend DNA. The A box interacts with residues 38-61 (TAD2) of the p53 transactivation domain. Residues 19-26 (TAD1) bind weakly, but only in the context of p53(1-93) and not as a free TAD1 peptide. We have solved the structure of the A-box/p53(1-93) complex by nuclear magnetic resonance spectroscopy. The incipient amphipathic helix in TAD2 recognizes the concave DNA-binding face of the A box and may be acting as a single-stranded DNA mimic.