CDGSH iron sulfur domain
From Wikipedia, the free encyclopedia
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| 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. | |
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CDGSH iron sulfur domain 1
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| Identifiers | |
| Symbol | CISD1 |
| Alt. Symbols | C10orf70, ZCD1 |
| Entrez | 55847 |
| HUGO | 30880 |
| PDB | 2QH7 |
| RefSeq | NM_018464 |
| UniProt | Q9NZ45 |
| Other data | |
| Locus | Chr. 10 q21.3 |
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CDGSH iron sulfur domain 1B
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| Identifiers | |
| Symbol | CISD1B |
| Alt. Symbols | ZCD1B |
| Entrez | 130500 |
| HUGO | 29611 |
| RefSeq | XM_065750 |
| Other data | |
| Locus | Chr. 2 p24.1 |
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CDGSH iron sulfur domain 2
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| Identifiers | |
| Symbol | CISD2 |
| Alt. Symbols | ZCD2 |
| Entrez | 493856 |
| HUGO | 24212 |
| RefSeq | NM_001008388 |
| UniProt | Q7Z3D5 |
| Other data | |
| Locus | Chr. 4 q24 |
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CDGSH iron sulfur domain 3
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| Identifiers | |
| Symbol | CISD3 |
| Entrez | 284106 |
| HUGO | 27578 |
| Other data | |
| Locus | Chr. 17 q12 |
The CDGSH iron sulfur domain are a group of iron-sulfur (Fe-S) 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]
[edit] References
- ^ 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. doi:. PMID 17766440.
- ^ 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:. PMID 14570702.
