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PDBsum entry 2ka6

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protein metals Protein-protein interface(s) links
Transcription regulator PDB id
2ka6
Jmol PyMol
Contents
Protein chains
92 a.a. *
45 a.a. *
Metals
_ZN ×3
* Residue conservation analysis
PDB id:
2ka6
Name: Transcription regulator
Title: Nmr structure of the cbp-taz2/stat1-tad complex
Structure: Creb-binding protein. Chain: a. Fragment: unp residues 1764 to 1855. Engineered: yes. Signal transducer and activator of transcription 1-alpha/beta. Chain: b. Fragment: unp residues 710 to 750. Synonym: transcription factor isgf-3 components p91/p84.
Source: Mus musculus. Mouse. Organism_taxid: 10090. Gene: cbp, crebbp. Expressed in: escherichia coli. Expression_system_taxid: 562. Homo sapiens. Human. Organism_taxid: 9606.
NMR struc: 20 models
Authors: J.M.Wojciak,M.A.Martinez-Yamout,H.J.Dyson,P.E.Wright
Key ref: J.M.Wojciak et al. (2009). Structural basis for recruitment of CBP/p300 coactivators by STAT1 and STAT2 transactivation domains. EMBO J, 28, 948-958. PubMed id: 19214187
Date:
30-Oct-08     Release date:   07-Apr-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P45481  (CBP_MOUSE) -  CREB-binding protein
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
2441 a.a.
92 a.a.
Protein chain
Pfam   ArchSchema ?
P42224  (STAT1_HUMAN) -  Signal transducer and activator of transcription 1-alpha/beta
Seq:
Struc:
 
Seq:
Struc:
750 a.a.
45 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chain A: E.C.2.3.1.48  - Histone acetyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Acetyl-CoA + [histone] = CoA + acetyl-[histone]
Acetyl-CoA
+ [histone]
= CoA
+ acetyl-[histone]
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     nucleus   1 term 
  Biological process     signal transduction   2 terms 
  Biochemical function     signal transducer activity     5 terms  

 

 
    Added reference    
 
 
EMBO J 28:948-958 (2009)
PubMed id: 19214187  
 
 
Structural basis for recruitment of CBP/p300 coactivators by STAT1 and STAT2 transactivation domains.
J.M.Wojciak, M.A.Martinez-Yamout, H.J.Dyson, P.E.Wright.
 
  ABSTRACT  
 
CBP/p300 transcriptional coactivators mediate gene expression by integrating cellular signals through interactions with multiple transcription factors. To elucidate the molecular and structural basis for CBP-dependent gene expression, we determined structures of the CBP TAZ1 and TAZ2 domains in complex with the transactivation domains (TADs) of signal transducer and activator of transcription 2 (STAT2) and STAT1, respectively. Despite the topological similarity of the TAZ1 and TAZ2 domains, subtle differences in helix packing and surface grooves constitute major determinants of target selectivity. Our results suggest that TAZ1 preferentially binds long TADs capable of contacting multiple surface grooves simultaneously, whereas smaller TADs that are restricted to a single contiguous binding surface form complexes with TAZ2. Complex formation for both STAT TADs involves coupled folding and binding, driven by intermolecular hydrophobic and electrostatic interactions. Phosphorylation of S727, required for maximal transcriptional activity of STAT1, does not enhance binding to any of the CBP domains. Because the different STAT TADs recognize different regions of CBP/p300, there is a potential for multivalent binding by STAT heterodimers that could enhance the recruitment of the coactivators to promoters.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21087945 A.Sebé-Pedrós, A.de Mendoza, B.F.Lang, B.M.Degnan, and I.Ruiz-Trillo (2011).
Unexpected Repertoire of Metazoan Transcription Factors in the Unicellular Holozoan Capsaspora owczarzaki.
  Mol Biol Evol, 28, 1241-1254.  
21268089 N.Li, R.C.Salter, and D.P.Ramji (2011).
Molecular mechanisms underlying the inhibition of IFN-γ-induced, STAT1-mediated gene transcription in human macrophages by simvastatin and agonists of PPARs and LXRs.
  J Cell Biochem, 112, 675-683.  
20962272 C.W.Lee, J.C.Ferreon, A.C.Ferreon, M.Arai, and P.E.Wright (2010).
Graded enhancement of p53 binding to CREB-binding protein (CBP) by multisite phosphorylation.
  Proc Natl Acad Sci U S A, 107, 19290-19295.  
21182795 J.D.Nardozzi, K.Lott, and G.Cingolani (2010).
Phosphorylation meets nuclear import: a review.
  Cell Commun Signal, 8, 32.  
20534573 M.L.Nelson, H.S.Kang, G.M.Lee, A.G.Blaszczak, D.K.Lau, L.P.McIntosh, and B.J.Graves (2010).
Ras signaling requires dynamic properties of Ets1 for phosphorylation-enhanced binding to coactivator CBP.
  Proc Natl Acad Sci U S A, 107, 10026-10031.
PDB code: 2kmd
19651603 J.C.Ferreon, M.A.Martinez-Yamout, H.J.Dyson, and P.E.Wright (2009).
Structural basis for subversion of cellular control mechanisms by the adenoviral E1A oncoprotein.
  Proc Natl Acad Sci U S A, 106, 13260-13265.
PDB code: 2kje
19966416 M.Miller, Z.Dauter, S.Cherry, J.E.Tropea, and A.Wlodawer (2009).
Structure of the Taz2 domain of p300: insights into ligand binding.
  Acta Crystallogr D Biol Crystallogr, 65, 1301-1308.
PDB code: 3io2
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 code is shown on the right.

 

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