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==Structure of the Mouse RNase H2 Complex== | ==Structure of the Mouse RNase H2 Complex== | ||
<StructureSection load='3kio' size='400' side='right' caption='mouse RNase H2 complex, (PDB code [[3kio]])> | <StructureSection load='3kio' size='400' side='right' caption='mouse RNase H2 complex, (PDB code [[3kio]])> | ||
+ | '''The RNase H2 ribonuclease complex''' is a heterotrimeric endoribonuclease responsible for the major ribonuclease H activity in mammalian cells. In mouse, the complex is encoded by 3 genes located on chromosomes 8 (Rnaseh2a), 14 (Rnaseh2b) and 19 (Rnaseh2c). This enzyme specifically cleaves the 3’O-Phosphate bond of RNA in a DNA/RNA hybrids to produce 5’ phosphate and 3’hydroxyl ends. | ||
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. |
Revision as of 21:31, 5 January 2015
This Sandbox is Reserved from 15/11/2014, through 15/05/2015 for use in the course "Biomolecule" taught by Bruno Kieffer at the Strasbourg University. This reservation includes Sandbox Reserved 951 through Sandbox Reserved 975. |
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Structure of the Mouse RNase H2 Complex
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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