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Cited by 1,759

The DOI matches its Crossref record.

Crystal Structure of the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase

Knighton, Daniel R., Zheng, Jianhua, Ten Eyck, Lynn F., Ashford, Victor A., Xuong, Nguyen-Huu, Taylor, Susan S., Sowadski, Janusz M.·1991·Science
DOI 10.1126/science.1862342
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Abstract

The crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase complexed with a 20-amino acid substrate analog inhibitor has been solved and partially refined at 2.7 Å resolution to an R factor of 0.212. The magnesium adenosine triphosphate (MgATP) binding site was located by difference Fourier synthesis. The enzyme structure is bilobal with a deep cleft between the lobes. The cleft is filled by MgATP and a portion of the inhibitor peptide. The smaller lobe, consisting mostly of amino-terminal sequence, is associated with nucleotide binding, and its largely antiparallel β sheet architecture constitutes an unusual nucleotide binding motif. The larger lobe is dominated by helical structure with a single β sheet at the domain interface. This lobe is primarily involved in peptide binding and catalysis. Residues 40 through 280 constitute a conserved catalytic core that is shared by more than 100 protein kinases. Most of the invariant amino acids in this conserved catalytic core are clustered at the sites of nucleotide binding and catalysis.

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Metadata

Authors
Knighton, D. R., Zheng, J., Ten Eyck, L. F., Ashford, V. A., Xuong, N.-H., Taylor, S. S., & Sowadski, J. M.
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
1991-07-26
Volume
253
Issue
5018
Pages
407-414
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
DOI
10.1126/science.1862342
OpenAlex
W2067405360
Cited by
1,759
References
0
FWCI
39.83
Type
journal article
Language
en
Open access
closed

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