Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3EGB

Structure of Pellino2 FHA domain at 3.3 Angstroms resolution.

Summary for 3EGB
Entry DOI10.2210/pdb3egb/pdb
Related3EGA
DescriptorProtein pellino homolog 2 (1 entity in total)
Functional Keywordspellino, fha domain, e3 ubiquitin ligase, substrate binding domain, phosphoprotein, protein binding
Biological sourceHomo sapiens (Human)
Total number of polymer chains2
Total formula weight62820.40
Authors
Ferguson, K.M.,Lin, C.,Schmitz, K.R. (deposition date: 2008-09-10, release date: 2008-12-23, Last modification date: 2023-08-30)
Primary citationLin, C.C.,Huoh, Y.S.,Schmitz, K.R.,Jensen, L.E.,Ferguson, K.M.
Pellino proteins contain a cryptic FHA domain that mediates interaction with phosphorylated IRAK1.
Structure, 16:1806-1816, 2008
Cited by
PubMed Abstract: Pellino proteins are RING E3 ubiquitin ligases involved in signaling events downstream of the Toll and interleukin-1 (IL-1) receptors, key initiators of innate immune and inflammatory responses. Pellino proteins associate with and ubiquitinate proteins in these pathways, including the interleukin-1 receptor associated kinase-1 (IRAK1). We determined the X-ray crystal structure of a Pellino2 fragment lacking only the RING domain. This structure reveals that the IRAK1-binding region of Pellino proteins consists largely of a previously unidentified forkhead-associated (FHA) domain. FHA domains are well-characterized phosphothreonine-binding modules, and this cryptic example in Pellino2 can drive interaction of this protein with phosphorylated IRAK1. The Pellino FHA domain is decorated with an unusual appendage or "wing" composed of two long inserts that lie within the FHA homology region. Delineating how this E3 ligase associates with substrates, and how these interactions are regulated by phosphorylation, is crucial for a complete understanding of Toll/IL-1 receptor signaling.
PubMed: 19081057
DOI: 10.1016/j.str.2008.09.011
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.25 Å)
Structure validation

229183

PDB entries from 2024-12-18

PDB statisticsPDBj update infoContact PDBjnumon