PDBsum entry 2jc2

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Metal binding protein PDB id
Protein chain
166 a.a. *
SO4 ×6
Waters ×140
* Residue conservation analysis
PDB id:
Name: Metal binding protein
Title: The crystal structure of the natural f112l human sorcin mutant
Structure: Sorcin. Chain: a, b, c, d. Synonym: 22 kda protein, cp-22, v19, f112l human sorcin mutant. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: heart, muscle, brain and adrenal medulla. Expressed in: escherichia coli. Expression_system_taxid: 469008.
2.50Å     R-factor:   0.254     R-free:   0.289
Authors: S.Franceschini,A.Ilari,G.Colotti,E.Chiancone
Key ref: S.Franceschini et al. (2008). Molecular basis for the impaired function of the natural F112L sorcin mutant: X-ray crystal structure, calcium affinity, and interaction with annexin VII and the ryanodine receptor. FASEB J, 22, 295-306. PubMed id: 17699613 DOI: 10.1096/fj.07-8988com
19-Dec-06     Release date:   28-Aug-07    
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Protein chains
Pfam   ArchSchema ?
P30626  (SORCN_HUMAN) -  Sorcin
198 a.a.
166 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     dendritic spine neck   19 terms 
  Biological process     positive regulation of insulin secretion involved in cellular response to glucose stimulus   23 terms 
  Biochemical function     ion channel binding     10 terms  


DOI no: 10.1096/fj.07-8988com FASEB J 22:295-306 (2008)
PubMed id: 17699613  
Molecular basis for the impaired function of the natural F112L sorcin mutant: X-ray crystal structure, calcium affinity, and interaction with annexin VII and the ryanodine receptor.
S.Franceschini, A.Ilari, D.Verzili, C.Zamparelli, A.Antaramian, A.Rueda, H.H.Valdivia, E.Chiancone, G.Colotti.
The penta-EF hand protein sorcin participates in the modulation of Ca2+-induced calcium-release in the heart through the interaction with several Ca2+ channels such as the ryanodine receptor. The modulating activity is impaired in the recently described natural F112L mutant. The F112 residue is located at the end of the D helix next to Asp113, one of the calcium ligands in the EF3 hand endowed with the highest affinity for the metal. The F112L-sorcin X-ray crystal structure at 2.5 A resolution displays marked alterations in the EF3 hand, where the hydrogen bonding network established by Phe112 is disrupted, and in the EF1 region, which is tilted in both monomers that give rise to the dimer, the stable form of the molecule. In turn, the observed tilt is indicative of an increased flexibility of the N-terminal part of the molecule. The structural alterations result in a 6-fold decrease in calcium affinity with respect to the wild-type protein and to an even larger impairment of the interaction with annexin VII and of the ability of sorcin to interact with and inhibit ryanodine receptors. These results provide a plausible structural and functional framework that helps elucidate the phenotypic alterations of mice overexpressing F112L-sorcin.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20298697 C.Zamparelli, N.Macquaide, G.Colotti, D.Verzili, T.Seidler, G.L.Smith, and E.Chiancone (2010).
Activation of the cardiac Na(+)-Ca(2+) exchanger by sorcin via the interaction of the respective Ca(2+)-binding domains.
  J Mol Cell Cardiol, 49, 132-141.  
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