User:Anthony Milto/Sandbox 1

From Proteopedia

MyoD

MyoD is a member of the basic helix loop helix (bHLH) family and myogenic factors subfamily of proteins. MyoD has a basic region at its amino-terminal end, which functions in binding the transcription factor to a region of the DNA known as the E-box. At its carboxyl-terminal end is MyoD's HLH domain. The HLH domain functions in protein-protein interactions and forms homodimeric and heterodimeric complexes. Differences in E-box sequences and in complex formation determine the transcription factor's effect and allow differentiation into a diverse array of muscle cells (REFERENCE). MyoD also contains an acidic activation domain. The activity of this activation domain has been observed to increase drastically upon deletion of residues in other parts of the protein. This suggests that the acidic activation domain is buried within the protein in vivo and can be activated by almost any change in structure. With this information, it has been proposed that DNA binding, with its accompanying structural changes, is the primary activator of MyoD (REFERENCE). MyoD's ability to activate endogenous genes has been shown to rely on two regions. The first is a region rich in cysteine and histidine residues that is between the acidic activation domain and the bHLH domain. The second is a region near the carboxyl terminus of the protein. These regions are conserved in proteins with shared functionality (REFERENCE).

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