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Figure 6
A comparison between SEPT2 and SEPT3 in the region of helix α5′. In SEPT3 (and all other subgroup members) helix α5′ is raised with respect to SEPT2 (which represents all of the remaining subgroups). This is a unique and consistent characteristic of the SEPT3 subgroup and its conformation is the result of a `characteristic' proline (Pro199) which alters the course of the polypeptide chain, including the polyacidic region (green). It is maintained by the hydrophobic contact between Ile281 (from α6) and Phe203 (from the polyacidic region), both of which are also characteristic of the SEPT3 subgroup. The residue numbers used apply to SEPT3.

Volume 7| Part 3| May 2020| Pages 462-479
ISSN: 2052-2525