NDLI: Crystal structure of the Alpha subunit PAS domain from soluble guanylyl cyclase

Content Provider	PubMed Central
Author	Purohit, Rahul Weichsel, Andrzej Montfort, William R.
Copyright Year	2013
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.
Related Links	http://dx.doi.org/10.1002/pro.2331
Ending Page	1444
Page Count	6
Starting Page	1439
File Format	PDF
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science : A Publication of the Protein Society
Issue Number	10
Volume Number	22
Language	English
Publisher	Blackwell Publishing Ltd
Publisher Date	2013-08-01
Access Restriction	Open
Rights Holder	Blackwell Publishing Ltd
Subject Keyword	Biochemistry Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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Crystal structure of the Alpha subunit PAS domain from soluble guanylyl cyclase