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Uncoupling conformational states from activity in an allosteric enzyme

Uncoupling conformational states from activity in an allosteric enzyme

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_603702800eb7417086645e28e6a8150e

Uncoupling conformational states from activity in an allosteric enzyme

About this item

Full title

Uncoupling conformational states from activity in an allosteric enzyme

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2017-08, Vol.8 (1), p.203-10, Article 203

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

ATP-phosphoribosyltransferase (ATP-PRT) is a hexameric enzyme in conformational equilibrium between an open and seemingly active state and a closed and presumably inhibited form. The structure-function relationship of allosteric regulation in this system is still not fully understood. Here, we develop a screening strategy for modulators of ATP-PRT...

Alternative Titles

Full title

Uncoupling conformational states from activity in an allosteric enzyme

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_603702800eb7417086645e28e6a8150e

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_603702800eb7417086645e28e6a8150e

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-017-00224-0

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