Structural insight to mutation effects uncover a common allosteric site in class C GPCRs | Zendy

Kasper Harpsøe | Zendy; Michael W. Boesgaard | Zendy; Christian Munk | Zendy; Hans BräunerOsborne | Zendy; David E. Gloriam | Zendy

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Structural insight to mutation effects uncover a common allosteric site in class C GPCRs

Author(s) -

Kasper Harpsøe,

Michael W. Boesgaard,

Christian Munk,

Hans BräunerOsborne,

David E. Gloriam

Publication year - 2016

Publication title -

bioinformatics

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.599

H-Index - 390

eISSN - 1367-4811

pISSN - 1367-4803

DOI - 10.1093/bioinformatics/btw784

Subject(s) - allosteric regulation , g protein coupled receptor , computational biology , mutation , class (philosophy) , genetics , computer science , biology , bioinformatics , artificial intelligence , receptor , gene

Class C G protein-coupled receptors (GPCRs) regulate important physiological functions and allosteric modulators binding to the transmembrane domain constitute an attractive and, due to a lack of structural insight, a virtually unexplored potential for therapeutics and the food industry. Combining pharmacological site-directed mutagenesis data with the recent class C GPCR experimental structures will provide a foundation for rational design of new therapeutics.

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