User:Abbas Raza/Sandbox 1
From Proteopedia
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NEIL3: a DNA repair glycosylase from mus musculus
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This protein is a unique member of family of DNA glysosylases, family of base excision repair enzymes that show preference for both oxidative purines and pyrimidine lesions. For a description of all known DNA glycosylases and their families see the wikepedia page on DNA glycosylases [[1]]. Originally identified through in-silico studies from Wallace, Mitra and Seeger group back in 2002(add reference), the crystallisation of neil3 remained challenge for almost a decade due to the difficulty in getting a stabilized form of the protein as it tend to aggregate until a truncated version was crystallised in 2013 and the crystal structure publlished (add reference).
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)
You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
Function
== Disease
Relevance
Structural highlights
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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
