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3brv
From Proteopedia
| 3brv, resolution 2.20Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Gene: | IKBKG, FIP3, NEMO (Homo sapiens) | ||||||||
| Activity: | I-kappa-B kinase, with EC number 2.7.11.10 | ||||||||
| Related: | 3brt | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
NEMO/IKKb association domain structure
The phosphorylation of IkappaB by the IKK complex targets it for degradation and releases NF-kappaB for translocation into the nucleus to initiate the inflammatory response, cell proliferation, or cell differentiation. The IKK complex is composed of the catalytic IKKalpha/beta kinases and a regulatory protein, NF-kappaB essential modulator (NEMO; IKKgamma). NEMO associates with the unphosphorylated IKK kinase C termini and activates the IKK complex's catalytic activity. However, detailed structural information about the NEMO/IKK interaction is lacking. In this study, we have identified the minimal requirements for NEMO and IKK kinase association using a variety of biophysical techniques and have solved two crystal structures of the minimal NEMO/IKK kinase associating domains. We demonstrate that the NEMO core domain is a dimer that binds two IKK fragments and identify energetic hot spots that can be exploited to inhibit IKK complex formation with a therapeutic agent.
Structure of a NEMO/IKK-Associating Domain Reveals Architecture of the Interaction Site., Rushe M, Silvian L, Bixler S, Chen LL, Cheung A, Bowes S, Cuervo H, Berkowitz S, Zheng T, Guckian K, Pellegrini M, Lugovskoy A, Structure. 2008 May;16(5):798-808. PMID:18462684
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
3BRV is a 4 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Rushe M, Silvian L, Bixler S, Chen LL, Cheung A, Bowes S, Cuervo H, Berkowitz S, Zheng T, Guckian K, Pellegrini M, Lugovskoy A. Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure. 2008 May;16(5):798-808. PMID:18462684 doi:10.1016/j.str.2008.02.012
Page seeded by OCA on Tue Feb 17 14:54:22 2009
Categories: Homo sapiens | I-kappa-B kinase | Silvian, L F. | Acetylation | Atp-binding | Coiled coil | Cytoplasm | Disease mutation | Ectodermal dysplasia | Fip3 | Host-virus interaction | Ikk-gamma | Ikkap1 | Kinase | Nemo | Nf-kb essential modulator | Nucleotide-binding | Nucleus | Phosphoprotein | Polymorphism | Serine/threonine-protein kinase | Transcription | Transcription regulation | Transferase | Transferase/transcription complex
