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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 2.2A 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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Rudolph MJ,Amodeo GA,Bai Y,Tong L

doi

10.1016/j.bbrc.2005.09.181

subject

Has Abstract

pub_date

2005-12-02 00:00:00

pages

1224-8

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)02205-9

journal_volume

337

pub_type

杂志文章

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