3UII

crystal structure of human Survivin in complex with H3(1-10) peptide

Summary for 3UII

• Entry DOI: 10.2210/pdb3uii/pdb
• Related: 3UIG 3UIH 3UIJ 3UIK
• Descriptor: Baculoviral IAP repeat-containing protein 5, histone H3(1-10) peptide, ZINC ION, ... (4 entities in total)
• Functional Keywords: bir domain, mitosis, t3 phosphorylated h3 binding, smac/diablo binding/h3 peptide, apoptosis-apoptosis inhibitor complex, apoptosis/apoptosis inhibitor
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: O15392
• Total number of polymer chains: 4
• Total formula weight: 35375.06

Authors

Du, J.,Patel, D.J. (deposition date: 2011-11-04, release date: 2012-02-01, Last modification date: 2023-09-13)

Primary citation

Du, J.,Kelly, A.E.,Funabiki, H.,Patel, D.J.
Structural Basis for Recognition of H3T3ph and Smac/DIABLO N-terminal Peptides by Human Survivin.
Structure, 20:185-195, 2012

PubMed Abstract: Survivin is an inhibitor of apoptosis family protein implicated in apoptosis and mitosis. In apoptosis, it has been shown to recognize the Smac/DIABLO protein. It is also a component of the chromosomal passenger complex, a key player during mitosis. Recently, Survivin was identified in vitro and in vivo as the direct binding partner for phosphorylated Thr3 on histone H3 (H3T3ph). We have undertaken structural and binding studies to investigate the molecular basis underlying recognition of H3T3ph and Smac/DIABLO N-terminal peptides by Survivin. Our crystallographic studies establish recognition of N-terminal Ala in both complexes and identify intermolecular hydrogen-bonding interactions in the Survivin phosphate-binding pocket that contribute to H3T3ph mark recognition. In addition, our calorimetric data establish that Survivin binds tighter to the H3T3ph-containing peptide relative to the N-terminal Smac/DIABLO peptide, and this preference can be reversed through structure-guided mutations that increase the hydrophobicity of the phosphate-binding pocket.

PubMed: 22244766
DOI: 10.1016/j.str.2011.12.001

Experimental method

X-RAY DIFFRACTION (2.6 Å)