top of page

Project Line 2: Heterodimerization Domain (HD)

The HD is a domain composed of around 160 amino acids that is furin cleaved at S1 into two non-covalently associated subunits.   It consists of an intimately intertwined α/β which fold around a conserved hydrophobic core.  Regulatory cleavage site S2 lies near the C-terminal end of the HD domain. (Figure 4)

 

Studies under this project line have been designed to answer the following questions:

Why do certain amino acid mutations in the HD cause cancer?

Is it because they:

  • Alter physiochemical properties?

  • Impact the secondary or tertiary structure?

  • Change the oligomerization state?

  • Affect protein stability?

  • Alter protein dynamics and accessibility?

You can find the progress on each question in the poster presentations of our undergraduate research team.

Figure 4: The LNR domain is shown as an opaque green molecular surface and the HD domain in the cartoon representation.  Structural elements N- and C-terminal to the S1 site are colored orange and purple respectively.  Residues with <10% solvent accessibility are shown in tan in their space filling models.

bottom of page