Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Architecture and activation of single-pass transmembrane receptor guanylyl cyclase.
Journal, issue, pages	Nat Struct Mol Biol, Year 2024
Publish date	Nov 14, 2024
Authors	Shian Liu / Alexander M Payne / Jinan Wang / Lan Zhu / Navid Paknejad / Edward T Eng / Wei Liu / Yinglong Miao / Richard K Hite / Xin-Yun Huang /
PubMed Abstract	The heart, in addition to its primary role in blood circulation, functions as an endocrine organ by producing cardiac hormone natriuretic peptides. These hormones regulate blood pressure through the ...The heart, in addition to its primary role in blood circulation, functions as an endocrine organ by producing cardiac hormone natriuretic peptides. These hormones regulate blood pressure through the single-pass transmembrane receptor guanylyl cyclase A (GC-A), also known as natriuretic peptide receptor 1. The binding of the peptide hormones to the extracellular domain of the receptor activates the intracellular guanylyl cyclase domain of the receptor to produce the second messenger cyclic guanosine monophosphate. Despite their importance, the detailed architecture and domain interactions within full-length GC-A remain elusive. Here we present cryo-electron microscopy structures, functional analyses and molecular dynamics simulations of full-length human GC-A, in both the absence and the presence of atrial natriuretic peptide. The data reveal the architecture of full-length GC-A, highlighting the spatial arrangement of its various functional domains. This insight is crucial for understanding how different parts of the receptor interact and coordinate during activation. The study elucidates the molecular basis of how extracellular signals are transduced across the membrane to activate the intracellular guanylyl cyclase domain.
External links	Nat Struct Mol Biol / PubMed:39543315
Methods	EM (single particle)
Resolution	2.9 - 7.82 Å
Structure data	44429 9bcl EMDB-44429, PDB-9bcl: Extracellular domain of apo GC-A, state 1 Method: EM (single particle) / Resolution: 2.9 Å EMDB-44430: Full-length apo GC-A Method: EM (single particle) / Resolution: 7.82 Å 44431 9bcn EMDB-44431, PDB-9bcn: Extracellular domain of apo GC-A, state 2 Method: EM (single particle) / Resolution: 2.9 Å 44432 9bco EMDB-44432, PDB-9bco: Intracellular domain of apo GC-A Method: EM (single particle) / Resolution: 4.4 Å 44433 9bcp EMDB-44433, PDB-9bcp: Kinase homology domain of apo GC-A Method: EM (single particle) / Resolution: 4.1 Å 44434 9bcq EMDB-44434, PDB-9bcq: Extracellular domain of GC-A bound to ANP Method: EM (single particle) / Resolution: 3.1 Å 44436 9bcs EMDB-44436, PDB-9bcs: Intracellular domain of GC-A bound to ANP Method: EM (single particle) / Resolution: 4.4 Å EMDB-44437: Full-length GC-A bound to ANP Method: EM (single particle) / Resolution: 7.4 Å 44440 9bcv EMDB-44440, PDB-9bcv: Cyclase domain of GC-A bound to ANP Method: EM (single particle) / Resolution: 3.2 Å
Chemicals	ChemComp-CL: Unknown entry ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM ChemComp-HOH: WATER ChemComp-G2P: PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER / GMP-CPP, energy-carrying molecule analogueYM ChemComp-MG: Unknown entry
Source	homo sapiens (human) mus musculus (house mouse)
Keywords	LYASE / Single pass transmembrane protein / guanylyl cyclase / atrial natriuretic peptide receptor / hypertension / membrane protein