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. Author manuscript; available in PMC: 2006 Mar 20.
Published in final edited form as: J Pept Res. 2005 Feb;65(2):209–220. doi: 10.1111/j.1399-3011.2005.00210.x

Figure 1.

Figure 1

Top panel shows a schematic of the kinesin-like heterotrimeric motor protein Kif3A/Kif3B/KAP3. This protein consists of two different polypeptide chains, Kif3A and Kif3B, which resemble conventional kinesin heavy chains. Each polypeptide chain contains a N-terminal globular motor domain, followed by a potential neck coiled-coil region, a highly charged hinge region, a coiled-coil stalk region and the C-terminal tail region (which binds to an accessory unit, the kinesin-like associated protein KAP3). Bottom panel shows the amino acid sequences of the complementary charged regions in Kif3A and Kif3B. Shown are the charged regions, residues 378–416 and 373–411, which comprise the non-homologous regions of Kif3A and Kif3B, respectively. The charged region of Kif3A begins with negatively charged amino acids followed by positively charged amino acids; the analogous region in Kif3B begins with a positively charged region followed by a glycine spacer and then a negatively charged region. CGG represents a flexible linker added N-terminally to each peptide. Ac-denotes Nα-acetyl and -amide denotes Cα-amide.