Figure 1.
Figure 1. (A) Cartoon representation of the structure of Ci-VSP. The N terminus of Ci-VSP spans four transmembrane segments forming the VSD, and the fourth segment (S4 segment) of the VSD is connected to the PD by the PBM. (B) The proposed PBM of Ci-VSP shares 50% identity with the first 16 amino acids of the PTEN. (C) Homology model of the PD of Ci-VSP. This homology model was created by the online package 3D-jigsaw using residues 240–576 of Ci-VSP (http:// bmm.cancerresearchuk.org/∼3djigsaw/). The obtained model comprises residues 253–574. (D) Crystal structure of PTEN. The crystal structure of PTEN is constituted by residues 14–351 (Lee et al., 1999). Arginines 253 and 254 of Ci-VSP (C) and 14 and 15 of PTEN (D) are displayed in red. These residues are implicated in the formation of the putative PBM in these proteins. Cysteine 363 of Ci-VSP and 124 in PTEN are displayed in blue. These residues are essential for the activity of the catalytic site.

(A) Cartoon representation of the structure of Ci-VSP. The N terminus of Ci-VSP spans four transmembrane segments forming the VSD, and the fourth segment (S4 segment) of the VSD is connected to the PD by the PBM. (B) The proposed PBM of Ci-VSP shares 50% identity with the first 16 amino acids of the PTEN. (C) Homology model of the PD of Ci-VSP. This homology model was created by the online package 3D-jigsaw using residues 240–576 of Ci-VSP (http:// bmm.cancerresearchuk.org/∼3djigsaw/). The obtained model comprises residues 253–574. (D) Crystal structure of PTEN. The crystal structure of PTEN is constituted by residues 14–351 (Lee et al., 1999). Arginines 253 and 254 of Ci-VSP (C) and 14 and 15 of PTEN (D) are displayed in red. These residues are implicated in the formation of the putative PBM in these proteins. Cysteine 363 of Ci-VSP and 124 in PTEN are displayed in blue. These residues are essential for the activity of the catalytic site.

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