User:Luke Edward Severinac/Sandbox 1

From Proteopedia

Revision as of 01:10, 2 April 2017

Caspase 6 in Homo Sapiens

spinqualitylabelsall models This is the 3D PDB protein that was presented in class, 4FXO. (Caspase-6) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image 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. This is the figure legend of the thumbnail Contents 1 Function 2 Structure 2.1 Active Site 2.2 Zinc Exoside 3 Activation of Caspase-6 3.1 Subunits involved in activation 3.2 Self cleavage 4 Inhbition 4.1 Zinc Inhibition 4.2 Phosphoylation 5 Luke's free space 6 Relevance Function Structure Active Site Caspase 6 is a part of the cystine aspartic protease family that cleaves proteins at the TEVD sequence. in its monomeric form with protein ligand bound, its catalytic residues are , , and . Cystine Aspartase mechanism Together, these residues form a that cleaves a . Zinc Exoside Activation of Caspase-6 Subunits involved in activation Self cleavage Inhbition Zinc Inhibition Phosphoylation Luke's free space If is , the activity of this protein is inhibited. If binds to the protein, the activity of the active site is inhibited. Inactive state of caspase 6: Relevance

References

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

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2966951/ (self cleavage article)

http://www.rcsb.org/pdb/explore/explore.do?structureId=2WDP (this is the non-self cleaved protien)