5AOQ

Structural basis of neurohormone perception by the receptor tyrosine kinase Torso

5AOQ の概要

• エントリーDOI: 10.2210/pdb5aoq/pdb
• 分子名称: TORSO, PREPROPTTH, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: transferase, ptth, prothoracicotropic hormone, metamorphosis, developmental timing, neurohormone, peptide hormone, cystine knot, receptor tyrosine kinase, rtk, fibronectin type iii domains, negative cooperativity
• 由来する生物種: BOMBYX MORI (DOMESTIC SILKWORM); 詳細
• 細胞内の位置: Cell membrane ; Single-pass type I membrane protein : D2IYS2
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 90032.74

構造登録者

Jenni, S.,Goyal, Y.,von Grotthuss, M.,Shvartsman, S.Y.,Klein, D.E. (登録日: 2015-09-11, 公開日: 2015-11-25, 最終更新日: 2020-07-29)

主引用文献

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

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: 26698662
DOI: 10.1016/J.MOLCEL.2015.10.026

実験手法

X-RAY DIFFRACTION (2.7 Å)