2CPK

CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CYCLIC ADENOSINE MONOPHOSPHATE-DEPENDENT PROTEIN KINASE

「1CPK」から置き換えられました

2CPK の概要

• エントリーDOI: 10.2210/pdb2cpk/pdb
• 分子名称: cAMP-DEPENDENT PROTEIN KINASE, CATALYTIC SUBUNIT, PEPTIDE INHIBITOR 20-MER (2 entities in total)
• 機能のキーワード: transferase(phosphotransferase)
• 由来する生物種: Mus musculus (house mouse); 詳細
• 細胞内の位置: Cytoplasm (By similarity): P05132
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 42963.71

構造登録者

Knighton, D.R.,Zheng, J.,Teneyck, L.F.,Ashford, V.A.,Xuong, N.-H.,Taylor, S.S.,Sowadski, J.M. (登録日: 1992-10-21, 公開日: 1993-01-15, 最終更新日: 2024-10-23)

主引用文献

Knighton, D.R.,Zheng, J.H.,Ten Eyck, L.F.,Ashford, V.A.,Xuong, N.H.,Taylor, S.S.,Sowadski, J.M.
Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase.
Science, 253:407-414, 1991

PubMed 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 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.

PubMed: 1862342

実験手法

X-RAY DIFFRACTION (2.7 Å)