1YTV

Maltose-binding protein fusion to a C-terminal fragment of the V1a vasopressin receptor

1YTV の概要

• エントリーDOI: 10.2210/pdb1ytv/pdb
• 関連するPDBエントリー: 1A7L
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: Maltose-binding periplasmic protein, Vasopressin V1a receptor, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: vasopressin; receptor; gpcr; fusion protein; maltose-binding protein, sugar binding protein, hormone receptor
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: P37288
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 100314.29

構造登録者

Adikesavan, N.V.,Mahmood, S.S.,Stanley, S.,Xu, Z.,Wu, N.,Thibonnier, M.,Shoham, M. (登録日: 2005-02-11, 公開日: 2005-04-12, 最終更新日: 2023-09-20)

主引用文献

Adikesavan, N.V.,Mahmood, S.S.,Stanley, N.,Xu, Z.,Wu, N.,Thibonnier, M.,Shoham, M.
A C-terminal segment of the V1R vasopressin receptor is unstructured in the crystal structure of its chimera with the maltose-binding protein.
Acta Crystallogr.,Sect.F, 61:341-345, 2005

PubMed Abstract: The V1 vascular vasopressin receptor (V1R) is a G-protein-coupled receptor (GPCR) involved in the regulation of body-fluid osmolality, blood volume and blood pressure. Signal transduction is mediated by the third intracellular loop of this seven-transmembrane protein as well as by the C-terminal cytoplasmic segment. A chimera of the maltose-binding protein (MBP) and the C-terminal segment of V1R has been cloned, expressed, purified and crystallized. The crystals belong to space group P2(1), with unit-cell parameters a = 51.10, b = 66.56, c = 115.72 A, beta = 95.99 degrees. The 1.8 A crystal structure reveals the conformation of MBP and part of the linker region of this chimera, with the C-terminal segment being unstructured. This may reflect a conformational plasticity in the C-terminal segment that may be necessary for proper function of V1R.

PubMed: 16511036
DOI: 10.1107/S1744309105007293

実験手法

X-RAY DIFFRACTION (1.8 Å)