1DGN
SOLUTION STRUCTURE OF ICEBERG, AN INHIBITOR OF INTERLEUKIN-1BETA GENERATION
Summary for 1DGN
| Entry DOI | 10.2210/pdb1dgn/pdb |
| Descriptor | ICEBERG (PROTEASE INHIBITOR) (1 entity in total) |
| Functional Keywords | antiparallel six-helix bundle, greek-key, hydrolase inhibitor |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 10023.68 |
| Authors | Humke, E.W.,Shriver, S.K.,Starovasnik, M.A.,Fairbrother, W.J.,Dixit, V.M. (deposition date: 1999-11-24, release date: 2000-10-09, Last modification date: 2024-05-22) |
| Primary citation | 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 Cited by 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: 11051551DOI: 10.1016/S0092-8674(00)00108-2 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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