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Crystal structures of the catalytic domain of human soluble guanylate cyclase

Crystal structures of the catalytic domain of human soluble guanylate cyclase

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1330881508

Crystal structures of the catalytic domain of human soluble guanylate cyclase

About this item

Full title

Crystal structures of the catalytic domain of human soluble guanylate cyclase

Publisher

United States: Public Library of Science

Journal title

PloS one, 2013-03, Vol.8 (3), p.e57644-e57644

Language

English

Formats

Publication information

Publisher

United States: Public Library of Science

More information

Scope and Contents

Contents

Soluble guanylate cyclase (sGC) catalyses the synthesis of cyclic GMP in response to nitric oxide. The enzyme is a heterodimer of homologous α and β subunits, each of which is composed of multiple domains. We present here crystal structures of a heterodimer of the catalytic domains of the α and β subunits, as well as an inactive homodimer of β subu...

Alternative Titles

Full title

Crystal structures of the catalytic domain of human soluble guanylate cyclase

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_plos_journals_1330881508

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1330881508

Other Identifiers

ISSN

1932-6203

E-ISSN

1932-6203

DOI

10.1371/journal.pone.0057644

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