1F3H

X-RAY CRYSTAL STRUCTURE OF THE HUMAN ANTI-APOPTOTIC PROTEIN SURVIVIN

Summary for 1F3H

• Entry DOI: 10.2210/pdb1f3h/pdb
• Descriptor: SURVIVIN, ZINC ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: apoptosis inhibitor survivin, thiol protease inhibitor, alpha-beta, apoptosis
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: O15392
• Total number of polymer chains: 2
• Total formula weight: 33284.55

Authors

Verdecia, M.A.,Huang, H.,Dutil, E.,Hunter, T.,Noel, J.P. (deposition date: 2000-06-03, release date: 2000-12-06, Last modification date: 2024-11-06)

Primary citation

Verdecia, M.A.,Huang, H.,Dutil, E.,Kaiser, D.A.,Hunter, T.,Noel, J.P.
Structure of the human anti-apoptotic protein survivin reveals a dimeric arrangement.
Nat.Struct.Biol., 7:602-608, 2000

PubMed Abstract: Survivin is a 16.5 kDa protein that is expressed during the G2/M phase of the cell cycle and is hypothesized to inhibit a default apoptotic cascade initiated in mitosis. This inhibitory function is coupled to survivin's localization to the mitotic spindle. To begin to address the structural basis of survivin's function, we report the X-ray crystal structure of a recombinant form of full length survivin to 2.58 A resolution. Survivin consists of two defined domains including an N-terminal Zn2+-binding BIR domain linked to a 65 A amphipathic C-terminal alpha-helix. The crystal structure reveals an extensive dimerization interface along a hydrophobic surface on the BIR domain of each survivin monomer. A basic patch acting as a sulfate/phosphate-binding module, an acidic cluster projecting off the BIR domain, and a solvent-accessible hydrophobic surface residing on the C-terminal amphipathic helix, are suggestive of functional protein-protein interaction surfaces.

PubMed: 10876248
DOI: 10.1038/77929

Experimental method

X-RAY DIFFRACTION (2.58 Å)