5L04
STRUCTURE OF INTERFERON LAMBDA 1 RECEPTOR WITH HUMAN KINASE JAK1
Summary for 5L04
| Entry DOI | 10.2210/pdb5l04/pdb |
| Descriptor | Tyrosine-protein kinase JAK1, Interferon lambda receptor 1 (3 entities in total) |
| Functional Keywords | complex of jak1 and interferon lambda 1, jak kinase, intracellular domain of ifnlr1, ferm domain, sh2-like domain, transferase-transferase inhibitor complex, transferase/transferase inhibitor |
| Biological source | Homo sapiens (Human) More |
| Cellular location | Endomembrane system; Peripheral membrane protein: P23458 Membrane ; Single-pass type I membrane protein : Q8IU57 |
| Total number of polymer chains | 2 |
| Total formula weight | 69430.31 |
| Authors | Lubkowski, J.,Wlodawer, A.,Zhang, D. (deposition date: 2016-07-26, release date: 2016-10-12, Last modification date: 2024-03-06) |
| Primary citation | Zhang, D.,Wlodawer, A.,Lubkowski, J. Crystal Structure of a Complex of the Intracellular Domain of Interferon lambda Receptor 1 (IFNLR1) and the FERM/SH2 Domains of Human JAK1. J. Mol. Biol., 428:4651-4668, 2016 Cited by PubMed Abstract: The crystal structure of a construct consisting of the FERM and SH2-like domains of the human Janus kinase 1 (JAK1) bound to a fragment of the intracellular domain of the interferon-λ receptor 1 (IFNLR1) has been determined at the nominal resolution of 2.1Å. In this structure, the receptor peptide forms an 85-Å-long extended chain, in which both the previously identified box1 and box2 regions bind simultaneously to the FERM and SH2-like domains of JAK1. Both domains of JAK1 are generally well ordered, with regions not seen in the crystal structure limited to loops located away from the receptor-binding regions. The structure provides a much more complete and accurate picture of the interactions between JAK1 and IFNLR1 than those given in earlier reports, illuminating the molecular basis of the JAK-cytokine receptor association. A glutamate residue adjacent to the box2 region in IFNLR1 mimics the mode of binding of a phosphotyrosine in classical SH2 domains. It was shown here that a deletion of residues within the box1 region of the receptor abolishes stable interactions with JAK1, although it was previously shown that box2 alone is sufficient to stabilize a similar complex of the interferon-α receptor and TYK2. PubMed: 27725180DOI: 10.1016/j.jmb.2016.10.005 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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