2K4P

Solution Structure of Ship2-Sam

2K4P の概要

• エントリーDOI: 10.2210/pdb2k4p/pdb
• 分子名称: Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2 (1 entity in total)
• 機能のキーワード: helix bundle, signaling protein, actin-binding, alternative splicing, cell adhesion, cytoplasm, cytoskeleton, diabetes mellitus, hydrolase, immune response, membrane, phosphoprotein, polymorphism, sh2 domain, sh3-binding
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm, cytosol: O15357
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9548.54

構造登録者

Leone, M.,Pellecchia, M. (登録日: 2008-06-16, 公開日: 2008-11-25, 最終更新日: 2024-05-29)

主引用文献

Leone, M.,Cellitti, J.,Pellecchia, M.
NMR Studies of a Heterotypic Sam-Sam Domain Association: The Interaction between the Lipid Phosphatase Ship2 and the EphA2 Receptor.
Biochemistry, 47:12721-12728, 2008

PubMed Abstract: Sterile alpha motif (Sam) domains are protein interaction modules that are implicated in many biological processes mainly via homo- and heterodimerization. It has been recently reported that the lipid phosphatase Ship2 regulates endocytosis of the EphA2 receptor, a process that has been investigated as a possible route to reduce tumor malignancy. A heterotypic Sam-Sam domain interaction is mediating this process. Here, we report NMR and ITC (isothermal titration calorimetry) studies on the Sam domain of Ship2 revealing its three-dimensional structure and its possible mode of interaction with the Sam domain from the EphA2 receptor. These studies have also resulted in the identification of a minimal peptide region of Ship2 that retains binding affinity for the Sam domain of the EphA2 receptor. Hence, this peptide and the detection of key structural elements important for EphA2 receptor endocytosis provide possible ways for the development of novel small molecule antagonists with potential anticancer activity.

PubMed: 18991394
DOI: 10.1021/bi801713f

実験手法

SOLUTION NMR