7KJO
crystal structure of PLEKHA7 PH domain biding SO4
Summary for 7KJO
| Entry DOI | 10.2210/pdb7kjo/pdb |
| Descriptor | Pleckstrin homology domain-containing family A member 7, SULFATE ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | plekha7, ph domain, pleckstrin homology domain, pip, inositol-phosphate, cell adhesion |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 32747.02 |
| Authors | Marassi, F.M.,Aleshin, A.E.,Liddington, R.C. (deposition date: 2020-10-26, release date: 2021-04-07, Last modification date: 2023-10-18) |
| Primary citation | Aleshin, A.E.,Yao, Y.,Iftikhar, A.,Bobkov, A.A.,Yu, J.,Cadwell, G.,Klein, M.G.,Dong, C.,Bankston, L.A.,Liddington, R.C.,Im, W.,Powis, G.,Marassi, F.M. Structural basis for the association of PLEKHA7 with membrane-embedded phosphatidylinositol lipids. Structure, 29:1029-, 2021 Cited by PubMed Abstract: PLEKHA7 (pleckstrin homology domain containing family A member 7) plays key roles in intracellular signaling, cytoskeletal organization, and cell adhesion, and is associated with multiple human cancers. The interactions of its pleckstrin homology (PH) domain with membrane phosphatidyl-inositol-phosphate (PIP) lipids are critical for proper cellular localization and function, but little is known about how PLEKHA7 and other PH domains interact with membrane-embedded PIPs. Here we describe the structural basis for recognition of membrane-bound PIPs by PLEHA7. Using X-ray crystallography, nuclear magnetic resonance, molecular dynamics simulations, and isothermal titration calorimetry, we show that the interaction of PLEKHA7 with PIPs is multivalent, distinct from a discrete one-to-one interaction, and induces PIP clustering. Our findings reveal a central role of the membrane assembly in mediating protein-PIP association and provide a roadmap for understanding how the PH domain contributes to the signaling, adhesion, and nanoclustering functions of PLEKHA7. PubMed: 33878292DOI: 10.1016/j.str.2021.03.018 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
Download full validation report
