2REA

Crystal structures of C2ALPHA-PI3 kinase PX-domain domain indicate conformational change associated with ligand binding.

2REA の概要

• エントリーDOI: 10.2210/pdb2rea/pdb
• 関連するPDBエントリー: 2ar5 2RED
• 分子名称: Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing alpha polypeptide (2 entities in total)
• 機能のキーワード: px domain, pi3k, kinase, transferase, phosphorylation, nuclear protein, phosphoinositide, cytoplasm, cytoplasmic vesicle, golgi apparatus, membrane, nucleus, polymorphism
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell membrane: O00443
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14375.57

構造登録者

Parkinson, G.N.,Vines, D.,Driscoll, P.C.,Djordjevic, S. (登録日: 2007-09-26, 公開日: 2007-11-27, 最終更新日: 2023-08-30)

主引用文献

Parkinson, G.N.,Vines, D.,Driscoll, P.C.,Djordjevic, S.
Crystal structures of PI3K-C2alpha PX domain indicate conformational change associated with ligand binding
Bmc Struct.Biol., 8:13-13, 2008

PubMed Abstract: PX domains have specialized protein structures involved in binding of phosphoinositides (PIs). Through binding to the various PIs PX domains provide site-specific membrane signals to modulate the intracellular localisation and biological activity of effector proteins. Several crystal structures of these domains are now available from a variety of proteins. All PX domains contain a canonical core structure with main differences exhibited within the loop regions forming the phosphoinositide binding pockets. It is within these areas that the molecular basis for ligand specificity originates.

PubMed: 18312637
DOI: 10.1186/1472-6807-8-13

実験手法

X-RAY DIFFRACTION (2.5 Å)