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2VFK

AKAP18 delta central domain - AMP

2VFK の概要
エントリーDOI10.2210/pdb2vfk/pdb
関連するPDBエントリー2VFL 2VFY
分子名称AKAP18 DELTA, ADENOSINE MONOPHOSPHATE (3 entities in total)
機能のキーワードapo, hydrolase
由来する生物種HOMO SAPIENS (HUMAN)
タンパク質・核酸の鎖数1
化学式量合計23574.16
構造登録者
Gold, M.G.,Smith, F.D.,Scott, J.D.,Barford, D. (登録日: 2007-11-05, 公開日: 2008-05-06, 最終更新日: 2024-05-01)
主引用文献Gold, M.G.,Smith, F.D.,Scott, J.D.,Barford, D.
Akap18 Contains a Phosphoesterase Domain that Binds AMP
J.Mol.Biol., 375:1329-, 2008
Cited by
PubMed Abstract: Protein kinase A anchoring proteins (AKAPs), defined by their capacity to target the cAMP-dependent protein kinase to distinct subcellular locations, function as molecular scaffolds mediating the assembly of multicomponent complexes to integrate and organise multiple signalling events. Despite their central importance in regulating cellular processes, little is known regarding their diverse structures and molecular mechanisms. Here, using bioinformatics and X-ray crystallography, we define a central domain of AKAP18 delta (AKAP18(CD)) as a member of the 2H phosphoesterase family. The domain features two conserved His-x-Thr motifs positioned at the base of a groove located between two lobes related by pseudo 2-fold symmetry. Nucleotide co-crystallisation screening revealed that this groove binds specifically to adenosine 5'-monophosphate (5'AMP) and cytosine 5'-monophosphate (5'CMP), with the affinity constant for AMP in the physiological concentration range. This is the first example of an AKAP capable of binding a small molecule. Our data generate two functional hypotheses for the AKAP18 central domain. It may act as a phosphoesterase, although we did not identify a substrate, or as an AMP sensor with the potential to couple intracellular AMP levels to PKA signalling events.
PubMed: 18082768
DOI: 10.1016/J.JMB.2007.11.037
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.5 Å)
構造検証レポート
Validation report summary of 2vfk
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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