Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:1.8
Classification:LYASE
Release Date:2013-08-14
Deposition Date:2012-08-09
Revision Date:2013-08-28#2013-10-09#2017-11-15
Molecular Weight:56341.24
Macromolecule Type:Protein
Residue Count:504
Atom Site Count:3676
DOI:10.2210/pdb4gj4/pdb
Abstract:
Soluble guanylate cyclase (sGC) is a heterodimeric heme protein of ≈ 150 kDa and the primary nitric oxide receptor. Binding of NO stimulates cyclase activity, leading to regulation of cardiovascular physiology and providing attractive opportunities for drug discovery. How sGC is stimulated and where candidate drugs bind remains unknown. The α and β sGC chains are each composed of Heme-Nitric Oxide Oxygen (H-NOX), Per-ARNT-Sim (PAS), coiled-coil and cyclase domains. Here, we present the crystal structure of the α1 PAS domain to 1.8 Å resolution. The structure reveals the binding surfaces of importance to heterodimer function, particularly with respect to regulating NO binding to heme in the β1 H-NOX domain. It also reveals a small internal cavity that may serve to bind ligands or participate in signal transduction.
Resolution:1.8
Classification:LYASE
Release Date:2013-08-14
Deposition Date:2012-08-09
Revision Date:2013-08-28#2013-10-09#2017-11-15
Molecular Weight:56341.24
Macromolecule Type:Protein
Residue Count:504
Atom Site Count:3676
DOI:10.2210/pdb4gj4/pdb
Abstract:
Soluble guanylate cyclase (sGC) is a heterodimeric heme protein of ≈ 150 kDa and the primary nitric oxide receptor. Binding of NO stimulates cyclase activity, leading to regulation of cardiovascular physiology and providing attractive opportunities for drug discovery. How sGC is stimulated and where candidate drugs bind remains unknown. The α and β sGC chains are each composed of Heme-Nitric Oxide Oxygen (H-NOX), Per-ARNT-Sim (PAS), coiled-coil and cyclase domains. Here, we present the crystal structure of the α1 PAS domain to 1.8 Å resolution. The structure reveals the binding surfaces of importance to heterodimer function, particularly with respect to regulating NO binding to heme in the β1 H-NOX domain. It also reveals a small internal cavity that may serve to bind ligands or participate in signal transduction.
| Date made available | 2013 |
|---|---|
| Publisher | RCSB-PDB |