Gene Ontology annotation through association of InterPro records with GO terms
Dimeric Structure of the Pseudokinase IRAK3 Suggests an Allosteric Mechanism for Negative Regulation.
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Human IRAK3 is a pseudokinase with a weak affinity for ATP and a closed pseudoactive conformation; its pseudokinase domain forms a dimer and interacts weakly with phosphorylated IRAK4 in native gels.
"In the case of IRAK3, elongated bands of IRAK3 and IRAK4-P indicate a weak interaction that causes IRAK3 to be dragged into the native gel, while delaying migration of IRAK4-P (lane 11)."
HORSE/IRAK3/IRAK3-bioinformatics/RESULTS.md
HORSE/IRAK3/IRAK3-bioinformatics/RESULTS-rereview.md
IRAK-M is a negative regulator of Toll-like receptor signaling.
IRAK-M is a novel member of the Pelle/interleukin-1 receptor-associated kinase (IRAK) family.