Production and Crystallization of Full-Length Human AMP-Activated Protein Kinase (α1β1γ1) View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

2018

AUTHORS

Julia A. Hubbard , Bing Xiao , Jon R. Wilson

ABSTRACT

Determination of the crystal structure of AMP-activated protein kinase (AMPK) is fundamental to understanding its biological function and role in a number of diseases related to energy metabolism including type 2 diabetes, obesity, and cancer. We describe methods for the expression and purification of a human full-length active AMPK complex that is suitable for biochemical and structural analyses, followed by methods for its crystallization in complex with small molecule activators. Quality control of the purified protein by functional and biophysical analysis was an essential part of the process enabling the achievement of crystals of the full-length protein capable of being used for high-resolution structure determination by X-ray diffraction. X-ray structures have been determined of both phosphorylated and non-phosphorylated forms of full-length human AMPK α1β1γ1. More... »

PAGES

1-14

Book

TITLE

AMPK

ISBN

978-1-4939-7597-6
978-1-4939-7598-3

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4939-7598-3_1

DOI

http://dx.doi.org/10.1007/978-1-4939-7598-3_1

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1101222274

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/29480465


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