User:Brian Ochoa/Sandbox 1
From Proteopedia
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== Function == | == Function == | ||
| - | BRCA1 is an 1,863 amino acid long protein that contains a ring finger motif from position 24 to 64. The ring motif is part of a larger domain spanning the first one hundred amino acid residues, which is required for the formation of its stable structure. This N-terminus domain is of the most highly conserved region of the BRCA1 gene and several cancer-predisposition mutations have been identified in this region. <ref>Meza, J. E., Brzovic, P. S., King, M., & Kelvin, R. E. (n.d.). Mapping the Functional Domains of BRCA1. Retrieved April 12, 2016, from http://www.jbc.org/content/274/9/5659.full#fn-5 | + | BRCA1 is an 1,863 amino acid long protein that contains a ring finger motif from position 24 to 64. The ring motif is part of a larger domain spanning the first one hundred amino acid residues, which is required for the formation of its stable structure. This N-terminus domain is of the most highly conserved region of the BRCA1 gene and several cancer-predisposition mutations have been identified in this region.<ref>Meza, J. E., Brzovic, P. S., King, M., & Kelvin, R. E. (n.d.). Mapping the Functional Domains of BRCA1. Retrieved April 12, 2016, from http://www.jbc.org/content/274/9/5659.full#fn-5 |
| - | doi: 10.1074/jbc.274.9.5659</ref> The ring motif is also a C3HC4 zinc-binding motif, named so for the conserved pattern of cysteine and histidines residues that bind the zinc ions (http://www.sciencedirect.com/science/article/pii/S0959440X96800601 | + | doi: 10.1074/jbc.274.9.5659</ref> The ring motif is also a C3HC4 zinc-binding motif, named so for the conserved pattern of cysteine and histidines residues that bind the zinc ions.<ref>Borden, K. L., & Freemont, P. S. (n.d.). The RING finger domain: A recent example of a sequence—structure family. Retrieved April 12, 2016, from http://www.sciencedirect.com/science/article/pii/S0959440X96800601 |
| + | doi:10.1016/S0959-440X(96)80060-1</ref> Ultimately, the ring motif of BRCA1 forms a heterodimer with the ring motif of BARD1 to assemble the functional protein complex. The solution structure of this complex shows that long alpha helices border the zinc binding residues in the ring motif. These alpha helices from the ring motif’s of BRCA1 and BARD1 combine to form a four-helix bundle that stabilizes the heterodimer and positions the zinc binding regions next to one another (http://www.jbc.org/content/274/9/5659.full). | ||
== Disease == | == Disease == | ||
Revision as of 22:18, 12 April 2016
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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
- ↑ Meza, J. E., Brzovic, P. S., King, M., & Kelvin, R. E. (n.d.). Mapping the Functional Domains of BRCA1. Retrieved April 12, 2016, from http://www.jbc.org/content/274/9/5659.full#fn-5 doi: 10.1074/jbc.274.9.5659
- ↑ Borden, K. L., & Freemont, P. S. (n.d.). The RING finger domain: A recent example of a sequence—structure family. Retrieved April 12, 2016, from http://www.sciencedirect.com/science/article/pii/S0959440X96800601 doi:10.1016/S0959-440X(96)80060-1
