8hbe
Structure of human soluble guanylate cyclase in the inactive state at 3.1 angstromStructure of human soluble guanylate cyclase in the inactive state at 3.1 angstrom
Structural highlights
DiseaseGCYA1_HUMAN Moyamoya disease with early-onset achalasia. The disease is caused by mutations affecting the gene represented in this entry. FunctionPublication Abstract from PubMedSoluble guanylate cyclase (sGC) is the primary receptor for nitric oxide (NO). The binding of NO to the haem of sGC induces a large conformational change in the enzyme and activates its cyclase activity. However, whether NO binds to the proximal site or the distal site of haem in the fully activated state remains under debate. Here, we present cryo-EM maps of sGC in the NO-activated state at high resolutions, allowing the observation of the density of NO. These cryo-EM maps show the binding of NO to the distal site of haem in the NO-activated state. NO binds to the distal site of haem in the fully activated soluble guanylate cyclase.,Liu R, Kang Y, Chen L Nitric Oxide. 2023 Mar 25;134-135:17-22. doi: 10.1016/j.niox.2023.03.002. PMID:36972843[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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