PDBsum entry 2e6w

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protein metals links
Metal binding protein PDB id
Jmol PyMol
Protein chain
96 a.a. *
_CA ×2
* Residue conservation analysis
PDB id:
Name: Metal binding protein
Title: Solution structure and calcium binding properties of ef- hands 3 and 4 of calsenilin
Structure: Calsenilin. Chain: a. Fragment: ef-hands 3 and 4. Synonym: dre-antagonist modulator, dream, kv channel- interacting protein 3, kchip3, a-type potassium channel modulatory protein 3. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: dream, kchip3. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
NMR struc: 1 models
Authors: L.Yu,C.Sun,R.Mendoza,E.Hebert,A.Pereda-Lopez,P.J.Hajduk, E.T.Olejniczak
Key ref:
L.Yu et al. (2007). Solution structure and calcium-binding properties of EF-hands 3 and 4 of calsenilin. Protein Sci, 16, 2502-2509. PubMed id: 17962406 DOI: 10.1110/ps.072928007
05-Jan-07     Release date:   27-Nov-07    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q9Y2W7  (CSEN_HUMAN) -  Calsenilin
256 a.a.
96 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     calcium ion binding     1 term  


DOI no: 10.1110/ps.072928007 Protein Sci 16:2502-2509 (2007)
PubMed id: 17962406  
Solution structure and calcium-binding properties of EF-hands 3 and 4 of calsenilin.
L.Yu, C.Sun, R.Mendoza, J.Wang, E.D.Matayoshi, E.Hebert, A.Pereda-Lopez, P.J.Hajduk, E.T.Olejniczak.
Calsenilin is a member of the recoverin branch of the EF-hand superfamily that is reported to interact with presenilins, regulate prodynorphin gene expression, modulate voltage-gated Kv4 potassium channel function, and bind to neurotoxins. Calsenilin is a Ca+2-binding protein and plays an important role in calcium signaling. Despite its importance in numerous neurological functions, the structure of this protein has not been reported. In the absence of Ca+2, the protein has limited spectral resolution that increases upon the addition of Ca+2. Here, we describe the three-dimensional solution structure of EF-hands 3 and 4 of calsenilin in the Ca+2-bound form. The Ca+2-bound structure consists of five alpha-helices and one two-stranded antiparallel beta-sheet. The long loop that connects EF hands 3 and 4 is highly disordered in solution. In addition to its structural effects, Ca+2 binding also increases the protein's propensity to dimerize. These changes in structure and oligomerization state induced upon Ca+2 binding may play important roles in molecular recognition during calcium signaling.
  Selected figure(s)  
Figure 6.
Figure 6. Molecular surfaces of calsenilin EF3--4 colored by local
Figure 7.
Figure 7. Ribbon plots comparing the structures of calsenilin EF3--4 (red)
  The above figures are reprinted by permission from the Protein Society: Protein Sci (2007, 16, 2502-2509) copyright 2007.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20680390 A.L.Getty, and D.A.Pearce (2011).
Interactions of the proteins of neuronal ceroid lipofuscinosis: clues to function.
  Cell Mol Life Sci, 68, 453-474.  
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