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. Author manuscript; available in PMC: 2014 Jan 1.
Published in final edited form as: Arch Biochem Biophys. 2012 Oct 24;529(1):18–25. doi: 10.1016/j.abb.2012.10.007

Figure 1. Sequence alignment of rat apoE and human apoE3 and apoE4.

Figure 1

The primary sequence of rat apoE was aligned with those of human apoE3 and apoE4 using the LALIGN program ((http://embnet.vital-it.ch/software/LALIGN_form.html) [45], which is available in ExPASy, the Swiss Institute of Bioinformatics Resource Portal (www.expasy.org). The only difference between the two human isoforms lies at position 112, which is a Cys in apoE3 and an Arg in apoE4 (bold). The corresponding site in rat apoE (position 104) is an Arg (bold). In apoE4, Arg61 (bold) is proposed to form a salt bridge with Glu255 (bold); in rat apoE, the corresponding position bears a Thr residue (bold) (Thr53). The sequence shown in blue for rat apoE is predicted to be the LDLr binding region, based on the known sites for human apoE3 and apoE4 (shown in red) [2]. Similarly, the predicted HSPG binding site in rat apoE (Lys135 and Lys138) are shown in bold, based on the known sites in human isoforms (Lys143 and Lys146).