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Title: Crystal Structure of the Protein Kinase Domain of Yeast AMP-Activated Protein Kinase Snf1

Abstract

AMP-activated protein kinase (AMPK) is a master metabolic regulator, and is an important target for drug development against diabetes, obesity, and other diseases. AMPK is a hetero-trimeric enzyme, with a catalytic ({alpha}) subunit, and two regulatory ({beta} and {gamma}) subunits. Here we report the crystal structure at 2.2 Angstrom resolution of the protein kinase domain (KD) of the catalytic subunit of yeast AMPK (commonly known as SNF1). The Snf1-KD structure shares strong similarity to other protein kinases, with a small N-terminal lobe and a large C-terminal lobe. Two negative surface patches in the structure may be important for the recognition of the substrates of this kinase.

Authors:
; ; ;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
913706
Report Number(s):
BNL-78274-2007-JA
Journal ID: ISSN 0006-291X; BBRCA9; TRN: US200804%%161
DOE Contract Number:
DE-AC02-98CH10886
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochem. Biophys. Res. Commun.; Journal Volume: 337
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE; CRYSTAL STRUCTURE; DISEASES; METABOLIC DISEASES; PHOSPHOTRANSFERASES; PROTEINS; RESOLUTION; SUBSTRATES; TARGETS; YEASTS; national synchrotron light source

Citation Formats

Rudolph,M., Amodeo, G., Bai, Y., and Tong, L. Crystal Structure of the Protein Kinase Domain of Yeast AMP-Activated Protein Kinase Snf1. United States: N. p., 2005. Web. doi:10.1016/j.bbrc.2005.09.181.
Rudolph,M., Amodeo, G., Bai, Y., & Tong, L. Crystal Structure of the Protein Kinase Domain of Yeast AMP-Activated Protein Kinase Snf1. United States. doi:10.1016/j.bbrc.2005.09.181.
Rudolph,M., Amodeo, G., Bai, Y., and Tong, L. 2005. "Crystal Structure of the Protein Kinase Domain of Yeast AMP-Activated Protein Kinase Snf1". United States. doi:10.1016/j.bbrc.2005.09.181.
@article{osti_913706,
title = {Crystal Structure of the Protein Kinase Domain of Yeast AMP-Activated Protein Kinase Snf1},
author = {Rudolph,M. and Amodeo, G. and Bai, Y. and Tong, L.},
abstractNote = {AMP-activated protein kinase (AMPK) is a master metabolic regulator, and is an important target for drug development against diabetes, obesity, and other diseases. AMPK is a hetero-trimeric enzyme, with a catalytic ({alpha}) subunit, and two regulatory ({beta} and {gamma}) subunits. Here we report the crystal structure at 2.2 Angstrom resolution of the protein kinase domain (KD) of the catalytic subunit of yeast AMPK (commonly known as SNF1). The Snf1-KD structure shares strong similarity to other protein kinases, with a small N-terminal lobe and a large C-terminal lobe. Two negative surface patches in the structure may be important for the recognition of the substrates of this kinase.},
doi = {10.1016/j.bbrc.2005.09.181},
journal = {Biochem. Biophys. Res. Commun.},
number = ,
volume = 337,
place = {United States},
year = 2005,
month = 1
}
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