User:Tanner Young/Sandbox 1: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
==Structure==
==Structure==


<scene name='78/786030/Pten/1'>PTEN</scene>  Alpha Helix and Beta pleated sheets
<scene name='78/786030/Pten/1'>PTEN</scene>  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).





Revision as of 19:17, 24 April 2018

StructureStructure

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).


This is a default text for your page Tanner Young/Sandbox 1. 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 [1] or to the article describing Jmol [2] to the rescue.

Function

PTEN is a dual phosphatase and tumor suppressor protein that interacts with LKB-1.

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.

Relevance

Structural highlights

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.


Caption for this structure

Drag the structure with the mouse to rotate

ReferencesReferences

  1. 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
  2. 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