CDGSH iron sulfur domain
Crystallographic structure (PDB: 2QH7​) of the CDGSH-type domain 1 dimer (green and cyan cartoon) complexed with iron (brown) and sulfur (yellow) Fe-S clusters.
Identifiers
SymbolCDGSH
PfamPF10660
InterProIPR019610
Membranome212
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
CDGSH iron sulfur domain 1
Identifiers
SymbolCISD1
Alt. symbolsC10orf70, ZCD1
NCBI gene55847
HGNC30880
PDB2QH7
RefSeqNM_018464
UniProtQ9NZ45
Other data
LocusChr. 10 q21.3
Search for
StructuresSwiss-model
DomainsInterPro
CDGSH iron sulfur domain 2
Identifiers
SymbolCISD2
Alt. symbolsZCD2
NCBI gene493856
HGNC24212
RefSeqNM_001008388
UniProtQ7Z3D5
Other data
LocusChr. 4 q24
Search for
StructuresSwiss-model
DomainsInterPro
CDGSH iron sulfur domain 3
Identifiers
SymbolCISD3
NCBI gene284106
HGNC27578
Other data
LocusChr. 17 q12

The CDGSH iron sulfur domain are a group of iron-sulfur (2Fe-2S) clusters and a unique 39 amino acid CDGSH domain [C-X-C-X2-(S/T)-X3-P-X-C-D-G-(S/A/T)-H].

The CDGSH iron sulfur domain 1 protein (also referred to as mitoNEET) is an integral membrane protein located in the outer mitochondrial membrane and whose function may be to transport iron into the mitochondria.[1] Iron in turn is essential for the function of several mitochondrial enzymes.

The antidiabetic drug pioglitazone, in addition to binding to the nuclear receptor PPAR, also has been shown to bind mitoNEET with approximately equal affinity.[2]

References

  1. ↑ Paddock ML, Wiley SE, Axelrod HL, Cohen AE, Roy M, Abresch EC, Capraro D, Murphy AN, Nechushtai R, Dixon JE, Jennings PA (2007). "MitoNEET is a uniquely folded 2Fe 2S outer mitochondrial membrane protein stabilized by pioglitazone". Proc. Natl. Acad. Sci. U.S.A. 104 (36): 14342–7. Bibcode:2007PNAS..10414342P. doi:10.1073/pnas.0707189104. PMC 1963346. PMID 17766440.
  2. ↑ Colca JR, McDonald WG, Waldon DJ, Leone JW, Lull JM, Bannow CA, Lund ET, Mathews WR (2004). "Identification of a novel mitochondrial protein ("mitoNEET") cross-linked specifically by a thiazolidinedione photoprobe". Am. J. Physiol. Endocrinol. Metab. 286 (2): E252–60. doi:10.1152/ajpendo.00424.2003. PMID 14570702.
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