User:Tanner Young/Sandbox 1
From Proteopedia
(Difference between revisions)
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== Function == | == Function == | ||
| - | PTEN is a dual phosphatase and tumor suppressor protein that interacts with LKB-1. | + | PTEN is a dual phosphatase and tumor suppressor protein that interacts with LKB-1. It is composed of a C-terminal and N-Terminal. The C-Terminal is a C2 Domain, this targets proteins to cell membranes. The N-terminal is a Phosphatase Domain, it’s job is to remove phosphate groups from a phosphorolated amino acid. |
== Disease == | == Disease == | ||
| - | The protein is located on the 10th chromosome 10q23.31 in humans. PTEN works with tumor suppressing for cancers, such as breast and prostate cancer. | + | The protein is located on the 10th chromosome 10q23.31 in humans. PTEN works with tumor suppressing for cancers, such as breast and prostate cancer. It also works to remove phosphate groups from specific amino acids, such as dephosphorylating tyrosine, serine, and threonine phosphorylated peptides. |
== Relevance == | == Relevance == | ||
Revision as of 16:24, 24 April 2018
Structure
is a protein that consists of 403-amino acids. Breaking it down into two main parts (the C-terminal and the N-terminal) it has 166 residues on the C-terminal (C2 Domain) and 179 on the N-terminal (Phosphatase Domain).
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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
