1WA9

Crystal Structure of the PAS repeat region of the Drosophila clock protein PERIOD

1WA9 の概要

• エントリーDOI: 10.2210/pdb1wa9/pdb
• 分子名称: PERIOD CIRCADIAN PROTEIN (2 entities in total)
• 機能のキーワード: period, pas domain, circadian rhythm, clock protein, phosphorylation, polymorphism
• 由来する生物種: DROSOPHILA MELANOGASTER (FRUIT FLY)
• 細胞内の位置: Nucleus: P07663
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 82914.94

構造登録者

Yildiz, O.,Doi, M.,Yujnovsky, I.,Cardone, L.,Berndt, A.,Hennig, S.,Schulze, S.,Urbanke, C.,Sassone-Corsi, P.,Wolf, E. (登録日: 2004-10-25, 公開日: 2005-01-12, 最終更新日: 2024-05-08)

主引用文献

Yildiz, O.,Doi, M.,Yujnovsky, I.,Cardone, L.,Berndt, A.,Hennig, S.,Schulze, S.,Urbanke, C.,Sassone-Corsi, P.,Wolf, E.
Crystal Structure and Interactions of the Pas Repeat Region of the Drosophila Clock Protein Period
Mol.Cell, 17:69-, 2005

PubMed Abstract: PERIOD proteins are central components of the Drosophila and mammalian circadian clock. Their function is controlled by daily changes in synthesis, cellular localization, phosphorylation, degradation, as well as specific interactions with other clock components. Here we present the crystal structure of a Drosophila PERIOD (dPER) fragment comprising two tandemly organized PAS (PER-ARNT-SIM) domains (PAS-A and PAS-B) and two additional C-terminal alpha helices (alphaE and alphaF). Our analysis reveals a noncrystallographic dPER dimer mediated by intermolecular interactions of PAS-A with PAS-B and helix alphaF. We show that alphaF is essential for dPER homodimerization and that the PAS-A-alphaF interaction plays a crucial role in dPER clock function, as it is affected by the 29 hr long-period perL mutation.

PubMed: 15629718
DOI: 10.1016/J.MOLCEL.2004.11.022

実験手法

X-RAY DIFFRACTION (3.15 Å)