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

التفاصيل البيبلوغرافية
العنوان: Crystal Structure of the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase
المؤلفون: L. F. Ten Eyck, Jianhua Zheng, Nguyen-Huu Xuong, Daniel R. Knighton, Susan S. Taylor, Victor A. Ashford, Janusz M. Sowadski
المصدر: Science. 253:407-414
بيانات النشر: American Association for the Advancement of Science (AAAS), 1991.
سنة النشر: 1991
مصطلحات موضوعية: Models, Molecular, chemistry.chemical_classification, Binding Sites, Multidisciplinary, Fourier Analysis, Macromolecular Substances, Stereochemistry, Protein subunit, Beta sheet, Peptide binding, Peptide, Recombinant Proteins, Enzyme structure, Mice, chemistry.chemical_compound, Adenosine Triphosphate, X-Ray Diffraction, chemistry, Animals, Computer Simulation, Cyclic adenosine monophosphate, Binding site, Protein kinase A, Protein Kinases
الوصف: 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 A 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 beta sheet architecture constitutes an unusual nucleotide binding motif. The larger lobe is dominated by helical structure with a single beta 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.
تدمد: 1095-9203
0036-8075
DOI: 10.1126/science.1862342
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c385b85908c0858e4a78cd9d4856332
https://doi.org/10.1126/science.1862342
رقم الانضمام: edsair.doi.dedup.....5c385b85908c0858e4a78cd9d4856332
قاعدة البيانات: OpenAIRE
الوصف
تدمد:10959203
00368075
DOI:10.1126/science.1862342