2K4P
Solution Structure of Ship2-Sam
Summary for 2K4P
| Entry DOI | 10.2210/pdb2k4p/pdb |
| Descriptor | Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2 (1 entity in total) |
| Functional Keywords | helix bundle, signaling protein, actin-binding, alternative splicing, cell adhesion, cytoplasm, cytoskeleton, diabetes mellitus, hydrolase, immune response, membrane, phosphoprotein, polymorphism, sh2 domain, sh3-binding |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm, cytosol: O15357 |
| Total number of polymer chains | 1 |
| Total formula weight | 9548.54 |
| Authors | Leone, M.,Pellecchia, M. (deposition date: 2008-06-16, release date: 2008-11-25, Last modification date: 2024-05-29) |
| Primary citation | 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 Cited by 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: 18991394DOI: 10.1021/bi801713f PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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