1F3H

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

1F3H の概要

• エントリーDOI: 10.2210/pdb1f3h/pdb
• 分子名称: SURVIVIN, ZINC ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: apoptosis inhibitor survivin, thiol protease inhibitor, alpha-beta, apoptosis
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: O15392
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 33284.55

構造登録者

Verdecia, M.A.,Huang, H.,Dutil, E.,Hunter, T.,Noel, J.P. (登録日: 2000-06-03, 公開日: 2000-12-06, 最終更新日: 2024-11-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.58 Å)