3LC8

Crystal structure of the cytoplasmic tail of (pro)renin receptor as a MBP fusion (Maltose-free form)

3LC8 の概要

• エントリーDOI: 10.2210/pdb3lc8/pdb
• 関連するPDBエントリー: 3LBS
• 分子名称: Maltose-binding periplasmic protein, Renin receptor, TETRAETHYLENE GLYCOL, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: renin receptor, prorenin receptor, atp6ap2, cytoplasmic tail, maltose binding protein fusion, sugar transport, transport, transport protein
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Membrane ; Single-pass type I membrane protein : O75787
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 85512.79

構造登録者

Zhang, Y.,Garavito, R.M. (登録日: 2010-01-10, 公開日: 2011-02-16, 最終更新日: 2023-09-06)

主引用文献

Zhang, Y.,Gao, X.,Michael Garavito, R.
Structural analysis of the intracellular domain of (pro)renin receptor fused to maltose-binding protein.
Biochem.Biophys.Res.Commun., 407:674-679, 2011

PubMed Abstract: The (pro)renin receptor (PRR) is an important component of the renin-angiotensin system (RAS), which regulates blood pressure and cardiovascular function. The integral membrane protein PRR contains a large extracellular domain (∼310 amino acids), a single transmembrane domain (∼20 amino acids) and an intracellular domain (∼19 amino acids). Although short, the intracellular (IC) domain of the PRR has functionally important roles in a number of signal transduction pathways activated by (pro)renin binding. Meanwhile, together with the transmembrane domain and a small portion of the extracellular domain (∼30 amino acids), the IC domain is also involved in assembly of V(0) portion of the vacuolar proton-translocating ATPase (V-ATPase). To better understand structural and multifunctional roles of the PRR-IC, we report the crystal structure of the PRR-IC domain as maltose-binding protein (MBP) fusion proteins at 2.0Å (maltose-free) and 2.15Å (maltose-bound). In the two separate crystal forms having significantly different unit-cell dimensions and molecular packing, MBP-PRR-IC fusion protein was found to be a dimer, which is different with the natural monomer of native MBP. The PRR-IC domain appears as a relatively flexible loop and is responsible for the dimerization of MBP fusion protein. Residues in the PRR-IC domain, particularly two tyrosines, dominate the intermonomer interactions, suggesting a role for the PRR-IC domain in protein oligomerization.

PubMed: 21420935
DOI: 10.1016/j.bbrc.2011.03.074

実験手法

X-RAY DIFFRACTION (2 Å)