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| <StructureSection load='3ag0' size='450' side='right' caption='Human cytoglobin including the heme group complex with CO (PDB code [[3ag0]])' scene='74/748876/Cv/1'> | | <StructureSection load='3ag0' size='350' side='right' caption='Human cytoglobin including the heme group complex with CO (PDB code [[3ag0]])' scene='74/748876/Cv/1'> |
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| == Function == | | == Function == |
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| == References == | | == References == |
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Revision as of 15:22, 19 October 2017
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Function
Cytoglobin (CYGB) is a globin which is ubiquitously expressed invertebrate tissues. CYGB is located in both cytoplasm and nucleus may provide O2 for enzymatic reactions and may be involved in NO-signaling pathways[1].
Disease
Loss of CYGB accelerates liver fibrosis and cancer development[2].
Structural highlights
CYGB heme group Fe has 6-fold coordination including the CO molecule as its 6th ligand[3]. Whole binding site.
- ↑ Ascenzi P, Bocedi A, de Sanctis D, Pesce A, Bolognesi M, Marden MC, Dewilde S, Moens L, Hankeln T, Burmester T. Neuroglobin and cytoglobin: Two new entries in the hemoglobin superfamily*. Biochem Mol Biol Educ. 2004 Sep;32(5):305-13. doi: 10.1002/bmb.2004.494032050386. PMID:21706744 doi:https://dx.doi.org/10.1002/bmb.2004.494032050386
- ↑ Thuy Le TT, Hai NT, Hai H, Kawada N. Pathophysiological role of cytoglobin, the fourth globin in mammals, in liver diseases. Histol Histopathol. 2016 Mar;31(3):257-67. doi: 10.14670/HH-11-694. Epub 2015 Nov, 11. PMID:26554615 doi:https://dx.doi.org/10.14670/HH-11-694
- ↑ Makino M, Sawai H, Shiro Y, Sugimoto H. Crystal structure of the carbon monoxide complex of human cytoglobin. Proteins. 2010 Nov 30. doi: 10.1002/prot.22950. PMID:21254233 doi:10.1002/prot.22950
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3D structures of cytoglobin
Updated on 19-October-2017
2dc3, 1v5h – hCYGB - human
1umo – hCYGB (mutant)
3ag0 – hCYGB + CO
1urv, 1ury, 1ut0, 1ux9 – hCYGB (mutant) + Fe(CN)6
4b3w – hCYGB (mutant) + CN + Fe(CN)6
References
