3SHR

Crystal Structure of cGMP-dependent Protein Kinase Reveals Novel Site of Interchain Communication

3SHR の概要

• エントリーDOI: 10.2210/pdb3shr/pdb
• 分子名称: cGMP-dependent protein kinase 1, ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE, SULFATE ION (3 entities in total)
• 機能のキーワード: cyclic nucleotide binding domains, cyclic nucleotide protein kinase, transferase, pkg, cgmp-dependent protein kinase
• 由来する生物種: Bos taurus (bovine,cow,domestic cattle,domestic cow)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 68211.47

構造登録者

Osborne, B.W.,Wu, J.,Taylor, S.S.,Dostmann, W.R. (登録日: 2011-06-16, 公開日: 2011-09-21, 最終更新日: 2026-03-04)

主引用文献

Osborne, B.W.,Wu, J.,McFarland, C.J.,Nickl, C.K.,Sankaran, B.,Casteel, D.E.,Woods, V.L.,Kornev, A.P.,Taylor, S.S.,Dostmann, W.R.
Crystal Structure of cGMP-Dependent Protein Kinase Reveals Novel Site of Interchain Communication.
Structure, 19:1317-1327, 2011

PubMed Abstract: The cGMP-dependent protein kinase (PKG) serves as an integral component of second messenger signaling in a number of biological contexts including cell differentiation, memory, and vasodilation. PKG is homodimeric and large conformational changes accompany cGMP binding. However, the structure of PKG and the molecular mechanisms associated with protomer communication following cGMP-induced activation remain unknown. Here, we report the 2.5 Å crystal structure of a regulatory domain construct (aa 78-355) containing both cGMP binding sites of PKG Iα. A distinct and segregated architecture with an extended central helix separates the two cGMP binding domains. Additionally, a previously uncharacterized helical domain (switch helix) promotes the formation of a hydrophobic interface between protomers. Mutational disruption of this interaction in full-length PKG implicates the switch helix as a critical site of dimer communication in PKG biology. These results offer new structural insight into the mechanism of allosteric PKG activation.

PubMed: 21893290
DOI: 10.1016/j.str.2011.06.012

実験手法

X-RAY DIFFRACTION (2.5 Å)