1DGN

SOLUTION STRUCTURE OF ICEBERG, AN INHIBITOR OF INTERLEUKIN-1BETA GENERATION

1DGN の概要

• エントリーDOI: 10.2210/pdb1dgn/pdb
• 分子名称: ICEBERG (PROTEASE INHIBITOR) (1 entity in total)
• 機能のキーワード: antiparallel six-helix bundle, greek-key, hydrolase inhibitor
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10023.68

構造登録者

Humke, E.W.,Shriver, S.K.,Starovasnik, M.A.,Fairbrother, W.J.,Dixit, V.M. (登録日: 1999-11-24, 公開日: 2000-10-09, 最終更新日: 2024-05-22)

主引用文献

Humke, E.W.,Shriver, S.K.,Starovasnik, M.A.,Fairbrother, W.J.,Dixit, V.M.
ICEBERG: a novel inhibitor of interleukin-1beta generation.
Cell(Cambridge,Mass.), 103:99-111, 2000

PubMed Abstract: ProIL-1beta is a proinflammatory cytokine that is proteolytically processed to its active form by caspase-1. Upon receipt of a proinflammatory stimulus, an upstream adaptor, RIP2, binds and oligomerizes caspase-1 zymogen, promoting its autoactivation. ICEBERG is a novel protein that inhibits generation of IL-1beta by interacting with caspase-1 and preventing its association with RIP2. ICEBERG is induced by proinflammatory stimuli, suggesting that it may be part of a negative feedback loop. Consistent with this, enforced retroviral expression of ICEBERG inhibits lipopolysaccharide-induced IL-1beta generation. The structure of ICEBERG reveals it to be a member of the death-domain-fold superfamily. The distribution of surface charge is complementary to the homologous prodomain of caspase-1, suggesting that charge-charge interactions mediate binding of ICEBERG to the prodomain of caspase-1.

PubMed: 11051551
DOI: 10.1016/S0092-8674(00)00108-2

実験手法

SOLUTION NMR