1JDN

Crystal Structure of Hormone Receptor

1JDN の概要

• エントリーDOI: 10.2210/pdb1jdn/pdb
• 関連するPDBエントリー: 1JDP
• 分子名称: ATRIAL NATRIURETIC PEPTIDE CLEARANCE RECEPTOR, beta-D-mannopyranose-(1-4)-alpha-D-mannopyranose-(1-4)-[beta-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose-(1-4)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: natriuretic peptide receptor, dimer, allosteric activation, signaling protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P17342
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 51580.50

構造登録者

He, X.-L.,Chow, D.-C.,Martick, M.M.,Garcia, K.C. (登録日: 2001-06-14, 公開日: 2001-09-05, 最終更新日: 2024-10-30)

主引用文献

He, X.l.,Chow, D.c.,Martick, M.M.,Garcia, K.C.
Allosteric activation of a spring-loaded natriuretic peptide receptor dimer by hormone.
Science, 293:1657-1662, 2001

PubMed Abstract: Natriuretic peptides (NPs) are vasoactive cyclic-peptide hormones important in blood pressure regulation through interaction with natriuretic cell-surface receptors. We report the hormone-binding thermodynamics and crystal structures at 2.9 and 2.0 angstroms, respectively, of the extracellular domain of the unliganded human NP receptor (NPR-C) and its complex with CNP, a 22-amino acid NP. A single CNP molecule is bound in the interface of an NPR-C dimer, resulting in asymmetric interactions between the hormone and the symmetrically related receptors. Hormone binding induces a 20 angstrom closure between the membrane-proximal domains of the dimer. In each monomer, the opening of an interdomain cleft, which is tethered together by a linker peptide acting as a molecular spring, is likely a conserved allosteric trigger for intracellular signaling by the natriuretic receptor family.

PubMed: 11533490
DOI: 10.1126/science.1062246

実験手法

X-RAY DIFFRACTION (2.9 Å)