3IM3

Crystal structure of PKA RI alpha dimerization/docking domain

3IM3 の概要

• エントリーDOI: 10.2210/pdb3im3/pdb
• 関連するPDBエントリー: 3IM4
• 分子名称: cAMP-dependent protein kinase type I-alpha regulatory subunit, FORMIC ACID (3 entities in total)
• 機能のキーワード: helix-turn-helix, acetylation, camp, camp-binding, disulfide bond, nucleotide-binding, phosphoprotein, structural protein, signaling protein
• 由来する生物種: Bos taurus (bovine)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6098.03

構造登録者

Sarma, G.N.,Kinderman, F.S.,Kim, C.,von Daake, S.,Taylor, S.S. (登録日: 2009-08-09, 公開日: 2010-02-02, 最終更新日: 2024-11-20)

主引用文献

Sarma, G.N.,Kinderman, F.S.,Kim, C.,von Daake, S.,Chen, L.,Wang, B.C.,Taylor, S.S.
Structure of D-AKAP2:PKA RI Complex: Insights into AKAP Specificity and Selectivity
Structure, 18:155-166, 2010

PubMed Abstract: A-kinase anchoring proteins (AKAPs) regulate cyclic AMP-dependent protein kinase (PKA) signaling in space and time. Dual-specific AKAP 2 (D-AKAP2) binds to the dimerization/docking (D/D) domain of both RI and RII regulatory subunits of PKA with high affinity. Here we have determined the structures of the RIalpha D/D domain alone and in complex with D-AKAP2. The D/D domain presents an extensive surface for binding through a well-formed N-terminal helix, and this surface restricts the diversity of AKAPs that can interact. The structures also underscore the importance of a redox-sensitive disulfide in affecting AKAP binding. An unexpected shift in the helical register of D-AKAP2 compared to the RIIalpha:D-AKAP2 complex structure makes the mode of binding to RIalpha novel. Finally, the comparison allows us to deduce a molecular explanation for the sequence and spatial determinants of AKAP specificity.

PubMed: 20159461
DOI: 10.1016/j.str.2009.12.012

実験手法

X-RAY DIFFRACTION (2 Å)