1R2A

THE MOLECULAR BASIS FOR PROTEIN KINASE A ANCHORING REVEALED BY SOLUTION NMR

1R2A の概要

• エントリーDOI: 10.2210/pdb1r2a/pdb
• NMR情報: BMRB: 4473
• 分子名称: PROTEIN (CAMP-DEPENDENT PROTEIN KINASE TYPE II REGULATORY SUBUNIT) (1 entity in total)
• 機能のキーワード: regulatory subunit, anchoring, four-helix bundle, transferase
• 由来する生物種: Mus musculus (house mouse)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 10796.36

構造登録者

Newlon, M.G.,Roy, M.,Morikis, D.,Hausken, Z.E.,Coghlan, V.,Scott, J.D.,Jennings, P.A. (登録日: 1998-12-07, 公開日: 1998-12-16, 最終更新日: 2023-12-27)

主引用文献

Newlon, M.G.,Roy, M.,Morikis, D.,Hausken, Z.E.,Coghlan, V.,Scott, J.D.,Jennings, P.A.
The molecular basis for protein kinase A anchoring revealed by solution NMR.
Nat.Struct.Biol., 6:222-227, 1999

PubMed Abstract: Compartmentalization of signal transduction enzymes into signaling complexes is an important mechanism to ensure the specificity of intracellular events. Formation of these complexes is mediated by specialized protein motifs that participate in protein-protein interactions. The adenosine 3',5'-cyclic monophosphate (cAMP)-dependent protein kinase (PKA) is localized through interaction of the regulatory (R) subunit dimer with A-kinase-anchoring proteins (AKAPs). We now report the solution structure of the type II PKA R-subunit fragment RIIalpha(1-44), which encompasses both the AKAP-binding and dimerization interfaces. This structure incorporates an X-type four-helix bundle dimerization motif with an extended hydrophobic face that is necessary for high-affinity AKAP binding. NMR data on the complex between RIIalpha(1-44) and an AKAP fragment reveals extensive contacts between the two proteins. Interestingly, this same dimerization motif is present in other signaling molecules, the S100 family. Therefore, the X-type four-helix bundle may represent a conserved fold for protein-protein interactions in signal transduction.

PubMed: 10074940
DOI: 10.1038/6663

実験手法

SOLUTION NMR