9TPI
Survivin 1-122 in complex with a molecular tweezer-Histone-H3-peptide conjugate
This is a non-PDB format compatible entry.
Summary for 9TPI
| Entry DOI | 10.2210/pdb9tpi/pdb |
| Descriptor | Baculoviral IAP repeat-containing protein 5, Histone-H3-peptide conjugated to molecular tweezer, ZINC ION, ... (6 entities in total) |
| Functional Keywords | protein-protein interactions, supramolecular ligands, molecular tweezers, peptide binding, bir domain, zinc finger, chromosomal passenger complex, cell cycle, mitosis, apoptosis |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 31125.69 |
| Authors | |
| Primary citation | Gsell, C.,Rebmann, P.,Opara, K.,Beuck, C.,Bayer, P.,Bier, D.,Vetter, I.R.,Schrader, T. Molecular tweezer-peptide conjugates disrupt the protein-protein interaction between survivin and histone H3 essential in mitosis. Beilstein J Org Chem, 22:557-567, 2026 Cited by PubMed Abstract: Peptide-modified supramolecular tweezers, a promising new class of chemical tools, were designed and employed to inhibit the interaction of the BIR domain of human survivin, a member of the chromosomal passenger complex (CPC), with the phosphorylated histone H3 N-terminal peptide. Fluorescence polarization measurements revealed a nanomolar affinity of the BIR domain for the peptide-tweezer, depending on the presence of lysine residue 121, as proven by the K121A mutant of survivin. Two crystal structures of C-terminally truncated human survivin with the peptide-tweezer molecules demonstrated that the peptide moiety binds the BIR domain as expected from the well-known published crystal structures of survivin with various peptides, but the tweezer itself, surprisingly, was bound to a putative Ca ion and the side chain of Pro26, corresponding to a previously unknown binding mode. Guided by the accessibility of survivin's lysine residues in the CPC, a number of new promising peptide tweezers was synthesized, able to connect both binding sites on the protein. PubMed: 41929663DOI: 10.3762/bjoc.22.41 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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