Fig. 1: Design of peptide-modified supramolecular tweezers.
From: Specific inhibition of the Survivin–CRM1 interaction by peptide-modified molecular tweezers
a Representation of Survivin’s dimer interface based on PDB-ID: 1XOX [https://www.rcsb.org/structure/1xox]38. Both monomers, depicted in blue and gray, mainly interact via the ELTL sequence (contact region of both monomers overlapping with the NES, represented in cyan and green). This sequence was chosen as second binding motif for the peptide-modified tweezer molecules. b Representation of TW-ELTL (shown in d) bound to Survivin. TW-ELTL (yellow) binds the anchor lysine residue K103 (violet) on Survivin’s surface while the peptide motif ELTL (yellow) interacts with the ELTL region of the Survivin monomer (cyan). This is the same region of the dimer interface represented in Fig. 1a, overlapping with the NES (cyan). The chemical structures of the unmodified tweezer molecule TW (c), an asymmetrical tweezer molecule linked to the short peptide ELTL (TW-ELTL) (d), and an asymmetrical tweezer molecule linked to the elongated peptide ELTLGEFL (TW-ELTLGEFL) (e) are depicted.
