3T4J
Arabidopsis histidine kinase 4 sensor domain in complex with N-isopentenyl adenine
Summary for 3T4J
Entry DOI | 10.2210/pdb3t4j/pdb |
Related | 3T4K 3T4L 3T4O 3T4Q 3T4S 3T4T |
Descriptor | Histidine kinase 4, N-(3-METHYLBUT-2-EN-1-YL)-9H-PURIN-6-AMINE, MALONATE ION, ... (4 entities in total) |
Functional Keywords | sensor histidine kinase, pas domain, family 1 sensor domain, hormone receptor, cytokinin binding, endoplasmic reticulum |
Biological source | Arabidopsis thaliana (mouse-ear cress,thale-cress) |
Cellular location | Cell membrane; Multi-pass membrane protein (By similarity): Q9C5U0 |
Total number of polymer chains | 2 |
Total formula weight | 61979.60 |
Authors | Hothorn, M. (deposition date: 2011-07-26, release date: 2011-10-05, Last modification date: 2024-10-09) |
Primary citation | Hothorn, M.,Dabi, T.,Chory, J. Structural basis for cytokinin recognition by Arabidopsis thaliana histidine kinase 4. Nat.Chem.Biol., 7:766-768, 2011 Cited by PubMed Abstract: Cytokinins are classic hormones that orchestrate plant growth and development and the integrity of stem cell populations. Cytokinin receptors are eukaryotic sensor histidine kinases that are activated by both naturally occurring adenine-type cytokinins and urea-based synthetic compounds. Crystal structures of the Arabidopsis thaliana histidine kinase 4 sensor domain in complex with different cytokinin ligands now rationalize the hormone-binding specificity of the receptor and may spur the design of new cytokinin ligands. PubMed: 21964459DOI: 10.1038/nchembio.667 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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