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Critical Features of Survivin Structure and Its Interaction Sites with Its Key Partners

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Martina Maritan

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Description: This figure is adapted from figure 3 of the article 'Survivin Small Molecule Inhibitors: Recent Advances and Challenges.' Survivin contains a BIR domain (18–88 aa), a linker region (89–102 aa), and a C-terminal α-helix (99–142 aa). Its N-terminal proline-rich sequence (first 10 aa) functions as a mitochondrial targeting sequence. The BIR domain interacts with Smac, Ran, XIAP, and HBXIP. The linker and N-terminal residues mediate dimerization, and the C-terminal forms a triple helix in the CPC.

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This figure is adapted from figure 3 of the article 'Survivin Small Molecule Inhibitors: Recent Advances and Challenges.' Survivin contains a BIR domain (18–88 aa), a linker region (89–102 aa), and a C-terminal α-helix (99–142 aa). Its N-terminal proline-rich sequence (first 10 aa) functions as a mitochondrial targeting sequence. The BIR domain interacts with Smac, Ran, XIAP, and HBXIP. The linker and N-terminal residues mediate dimerization, and the C-terminal forms a triple helix in the CPC.

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