User:Abbas Raza/Sandbox 1
From Proteopedia
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[[Image:neil3 full structure.png|thumb|left|300px|mouse neil3]] | [[Image:neil3 full structure.png|thumb|left|300px|mouse neil3]] | ||
<StructureSection load='3wOf' size='340' side='right' caption='Crystal structure representation of neil3' scene=''> | <StructureSection load='3wOf' size='340' side='right' caption='Crystal structure representation of neil3' scene=''> | ||
| + | This protein is a unique member of Fpg/NEIL family of DNA glysosylases which shows preference for both oxidative purines and pyrimidine lesions. Originally identified through in-silico studies from Wallace, Mitra and Seeger group back in 2002, the crystallisation of NEIL3 remained challenge for almost a decade due to the difficulty in getting fulll length purification of the protein as it tend to aggregate until a trancated version was crystallised in 2013 and the crystal structure publlished. | ||
| + | Neil3 proteins are almost twice the size of other Fpg/Nei family members. The N terminus of the Neil3 proteins is highly conserved, with a complete Fpg/Nei-like core protein that harbors an H2TH motif and a canonical zinc finger motif. Neil3 proteins also have a Ran binding protein (RanBP2)-type zinc finger motif and a duplicated GRF-zinc finger motif at their extended C terminus (Bandaru et al., 2002; Krokeide et al., 2009; Liu et al., 2010; Morland et al., 2002; Takao et al., 2009; Torisu et al., 2005) | ||
Revision as of 00:15, 25 April 2014
Neil3: a DNA repair glycosylase from mus musculus
Image:Neil3 full structure.png
mouse neil3
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
