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PDBsum entry 2jul

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protein metals links
DNA binding protein PDB id
2jul
Jmol
Contents
Protein chain
181 a.a. *
Metals
_CA ×2
* Residue conservation analysis
PDB id:
2jul
Name: DNA binding protein
Title: Nmr structure of dream
Structure: Calsenilin. Chain: a. Synonym: kv channel-interacting protein 3, kchip3, a-type potassium channel modulatory protein 3, dre-antagonist modulator, dream. Engineered: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Gene: kcnip3, csen, dream, kchip3. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
NMR struc: 15 models
Authors: J.Ames
Key ref: J.D.Lusin et al. (2008). NMR structure of DREAM: Implications for Ca(2+)-dependent DNA binding and protein dimerization. Biochemistry, 47, 2252-2264. PubMed id: 18201103 DOI: 10.1021/bi7017267
Date:
30-Aug-07     Release date:   22-Apr-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9QXT8  (CSEN_MOUSE) -  Calsenilin
Seq:
Struc:
256 a.a.
181 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     protein-DNA complex   11 terms 
  Biological process     potassium ion transmembrane transport   15 terms 
  Biochemical function     ion channel binding     10 terms  

 

 
DOI no: 10.1021/bi7017267 Biochemistry 47:2252-2264 (2008)
PubMed id: 18201103  
 
 
NMR structure of DREAM: Implications for Ca(2+)-dependent DNA binding and protein dimerization.
J.D.Lusin, M.Vanarotti, C.Li, A.Valiveti, J.B.Ames.
 
  ABSTRACT  
 
DREAM (calsenilin/KChIP3) is an EF-hand calcium-binding protein that binds to specific DNA sequences and regulates Ca2+-induced transcription of prodynorphin and c-fos genes. Here, we present the atomic-resolution structure of Ca2+-bound DREAM in solution determined by nuclear magnetic resonance (NMR) spectroscopy. Pulsed-field gradient NMR diffusion experiments and 15N NMR relaxation analysis indicate that Ca2+-bound DREAM forms a stable dimer in solution. The structure of the first 77 residues from the N-terminus could not be determined by our NMR analysis. The C-terminal DREAM structure (residues 78-256) contains four EF-hand motifs arranged in a tandem linear array, similar to that seen in KChIP1, recoverin, and other structures of the neuronal calcium sensor (NCS) branch of the calmodulin superfamily. Mg2+ is bound at the second EF-hand, whereas Ca2+ is bound functionally at the third and fourth sites. The first and second EF-hands form an exposed hydrophobic groove on the protein surface lined by side-chain atoms of L96, F100, F114, I117, Y118, F121, F122, Y151, L155, L158, and L159 that are highly conserved in all NCS proteins. An exposed leucine near the C-terminus (L251) is suggested to form intermolecular contacts with leucine residues in the hydrophobic groove (L155, L158, and L159). Positively charged side chains of Arg and Lys (Lys87, Lys90, Lys91, Arg98, Lys101, Arg160, and Lys166) are clustered on one side of the protein surface and may mediate electrostatic contacts with DNA targets. We propose that Ca2+-induced dimerization of DREAM may partially block the putative DNA-binding site, which may suggest as to how Ca2+ abolishes DREAM binding to DNA to activate the transcription of prodynorphin and other downstream genes in pain control.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21070824 M.Palczewska, I.Casafont, K.Ghimire, A.M.Rojas, A.Valencia, M.Lafarga, B.Mellström, and J.R.Naranjo (2011).
Sumoylation regulates nuclear localization of repressor DREAM.
  Biochim Biophys Acta, 1813, 1050-1058.  
20154682 D.Anderson, W.H.Mehaffey, M.Iftinca, R.Rehak, J.D.Engbers, S.Hameed, G.W.Zamponi, and R.W.Turner (2010).
Regulation of neuronal activity by Cav3-Kv4 channel signaling complexes.
  Nat Neurosci, 13, 333-337.  
19238593 M.Vallejo (2009).
PACAP signaling to DREAM: A cAMP-Dependent Pathway that Regulates Cortical Astrogliogenesis.
  Mol Neurobiol, 39, 90.  
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.