5AOQ
Structural basis of neurohormone perception by the receptor tyrosine kinase Torso
Summary for 5AOQ
| Entry DOI | 10.2210/pdb5aoq/pdb |
| Descriptor | TORSO, PREPROPTTH, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
| Functional Keywords | transferase, ptth, prothoracicotropic hormone, metamorphosis, developmental timing, neurohormone, peptide hormone, cystine knot, receptor tyrosine kinase, rtk, fibronectin type iii domains, negative cooperativity |
| Biological source | BOMBYX MORI (DOMESTIC SILKWORM) More |
| Cellular location | Cell membrane ; Single-pass type I membrane protein : D2IYS2 |
| Total number of polymer chains | 4 |
| Total formula weight | 90032.74 |
| Authors | Jenni, S.,Goyal, Y.,von Grotthuss, M.,Shvartsman, S.Y.,Klein, D.E. (deposition date: 2015-09-11, release date: 2015-11-25, Last modification date: 2024-11-13) |
| Primary citation | Jenni, S.,Goyal, Y.,von Grotthuss, M.,Shvartsman, S.Y.,Klein, D.E. Structural Basis of Neurohormone Perception by the Receptor Tyrosine Kinase Torso. Mol.Cell, 60:941-, 2015 Cited by PubMed Abstract: In insects, brain-derived Prothoracicotropic hormone (PTTH) activates the receptor tyrosine kinase (RTK) Torso to initiate metamorphosis through the release of ecdysone. We have determined the crystal structure of silkworm PTTH in complex with the ligand-binding region of Torso. Here we show that ligand-induced Torso dimerization results from the sequential and negatively cooperative formation of asymmetric heterotetramers. Mathematical modeling of receptor activation based upon our biophysical studies shows that ligand pulses are "buffered" at low receptor levels, leading to a sustained signal. By contrast, high levels of Torso develop the signal intensity and duration of a noncooperative system. We propose that this may allow Torso to coordinate widely different functions from a single ligand by tuning receptor levels. Phylogenic analysis indicates that Torso is found outside arthropods, including human parasitic roundworms. Together, our findings provide mechanistic insight into how this receptor system, with roles in embryonic and adult development, is regulated. PubMed: 26698662DOI: 10.1016/J.MOLCEL.2015.10.026 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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