1E31

SURVIVIN DIMER H. SAPIENS

Summary for 1E31

• Entry DOI: 10.2210/pdb1e31/pdb
• Descriptor: APOPTOSIS INHIBITOR SURVIVIN, ZINC ION, COBALT (II) ION, ... (4 entities in total)
• Functional Keywords: apoptosis inhibitor, iap, apotosis, zinc finger
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasm: O15392
• Total number of polymer chains: 2
• Total formula weight: 33019.22

Authors

Chantalat, L.,Skoufias, D.A.,Margolis, R.L.,Dideberg, O. (deposition date: 2000-06-04, release date: 2001-01-03, Last modification date: 2024-05-08)

Primary citation

Chantalat, L.,Skoufias, D.A.,Kleman, J.P.,Jung, B.,Dideberg, O.,Margolis, R.L.
Crystal Structure of Human Survivin Reveals a Bow Tie-Shaped Dimer with Two Unusual Alpha-Helical Extensions
Mol.Cell, 6:183-, 2000

PubMed Abstract: Survivin is a mitotic spindle-associated protein involved in linking mitotic spindle function to activation of apoptosis in mammalian cells. The structure of the full-length human survivin has been determined by X-ray crystallography to 2.7 A. Strikingly, the structure forms a very unusual bow tie-shaped dimer. It does not dimerize through a C-terminal coiled-coil, contrary to sequence analysis prediction. The C-terminal helices contain hydrophobic clusters with the potential for protein-protein interactions. The unusual shape and dimensions of survivin suggest it serves an adaptor function through its alpha-helical extensions.

PubMed: 10949039
DOI: 10.1016/S1097-2765(00)00019-8

Experimental method

X-RAY DIFFRACTION (2.71 Å)