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. Author manuscript; available in PMC: 2016 Oct 31.
Published in final edited form as: Clin Genet. 2010 Feb 11;77(6):511–524. doi: 10.1111/j.1399-0004.2010.01392.x

Figure 2. General structure of septins.

Figure 2

N- and C- termini vary between Septin family members and their isoforms. Some septins contain a proline rich domain in their amino terminus that is involved in protein interaction. The C- terminus of some septins consists of a coiled-coil domain predicted to contain a α-helix. The polybasic domain is responsible for the association of septins with the plasma membrane. The central GTP-binding domain contains conserved motifs G1 (GxxxxGK[S/T]), G3 (DxxG) and G4 (xKxD) and is implicated in the formation of septin heteroligomers and protein interaction.