2A9I
Molecular Structure of the Interleukin-1 Receptor-Associated Kinase-4 Death Domain
Summary for 2A9I
Entry DOI | 10.2210/pdb2a9i/pdb |
Descriptor | Interleukin-1 receptor-associated kinase-4, MANGANESE (II) ION (3 entities in total) |
Functional Keywords | hexahelical bundle, transferase |
Biological source | Mus musculus (house mouse) |
Total number of polymer chains | 1 |
Total formula weight | 12719.59 |
Authors | Lasker, M.V.,Gajjar, M.M.,Nair, S.K. (deposition date: 2005-07-11, release date: 2005-10-11, Last modification date: 2024-02-14) |
Primary citation | Lasker, M.V.,Gajjar, M.M.,Nair, S.K. Cutting Edge: Molecular Structure of the IL-1R-Associated Kinase-4 Death Domain and Its Implications for TLR Signaling. J.Immunol., 175:4175-4179, 2005 Cited by PubMed Abstract: IL-1R-associated kinase (IRAK) 4 is an essential component of innate immunity. IRAK-4 deficiency in mice and humans results in severe impairment of IL-1 and TLR signaling. We have solved the crystal structure for the death domain of Mus musculus IRAK-4 to 1.7 A resolution. This is the first glimpse of the structural details of a mammalian IRAK family member. The crystal structure reveals a six-helical bundle with a prominent loop, which among IRAKs and Pelle, a Drosophila homologue, is unique to IRAK-4. This highly structured loop contained between helices two and three, comprises an 11-aa stretch. Although innate immune domain recognition is thought to be very similar between Drosophila and mammals, this structural component points to a drastic difference. This structure can be used as a framework for future mutation and deletion studies and potential drug design. PubMed: 16177054PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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