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. Author manuscript; available in PMC: 2010 Jul 1.
Published in final edited form as: Trends Cardiovasc Med. 2009 Jul;19(5):173–177. doi: 10.1016/j.tcm.2009.10.003

Figure 2.

Figure 2

Oligomerization of HMGCR catalytic domains. The catalytic domain of the classical HMGCR enzyme, HMGCR13(+), has been shown to exist as a tetramer comprised of two dimers (Istvan et al. 2000). This conformation is fully active and sensitive to competition inhibition by statins. Although evidence suggests that deletion of exon 13 abolishes HMGCR enzymatic activity (Burkhardt et al. 2008), these studies did not consider the possibility that the 13(+) and 13(−) monomers may form heterogenous dimers or tetramers comprised of varying compositions of the 13(+) and 13(−) monomers. In the context of these hypothetical conformations, 13(−) may attenuate HMGCR enzyme activity and statin sensitivity, consistent with our reports that modulating the relative levels of the 13(+) to 13(−) transcript alters the statin sensitivity of the resulting HMGCR enzyme.