7AAM
Crystal structure of the F-BAR domain of PSTIPIP1 bound to the CTH domain of the phosphatase LYP
Summary for 7AAM
| Entry DOI | 10.2210/pdb7aam/pdb |
| Related | 7AAL 7AAN |
| Descriptor | Proline-serine-threonine phosphatase-interacting protein 1, Tyrosine-protein phosphatase non-receptor type 22, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | pyogenic arthritis, pyoderma gangrenosum and acne (papa), inflammatory response, membrane binding, signaling protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 3 |
| Total formula weight | 71090.97 |
| Authors | Manso, J.A.,Alcon, P.,Bayon, Y.,Alonso, A.,de Pereda, J.M. (deposition date: 2020-09-04, release date: 2022-02-23, Last modification date: 2024-02-07) |
| Primary citation | Manso, J.A.,Marcos, T.,Ruiz-Martin, V.,Casas, J.,Alcon, P.,Sanchez Crespo, M.,Bayon, Y.,de Pereda, J.M.,Alonso, A. PSTPIP1-LYP phosphatase interaction: structural basis and implications for autoinflammatory disorders. Cell.Mol.Life Sci., 79:131-131, 2022 Cited by PubMed Abstract: Mutations in the adaptor protein PSTPIP1 cause a spectrum of autoinflammatory diseases, including PAPA and PAMI; however, the mechanism underlying these diseases remains unknown. Most of these mutations lie in PSTPIP1 F-BAR domain, which binds to LYP, a protein tyrosine phosphatase associated with arthritis and lupus. To shed light on the mechanism by which these mutations generate autoinflammatory disorders, we solved the structure of the F-BAR domain of PSTPIP1 alone and bound to the C-terminal homology segment of LYP, revealing a novel mechanism of recognition of Pro-rich motifs by proteins in which a single LYP molecule binds to the PSTPIP1 F-BAR dimer. The residues R228, D246, E250, and E257 of PSTPIP1 that are mutated in immunological diseases directly interact with LYP. These findings link the disruption of the PSTPIP1/LYP interaction to these diseases, and support a critical role for LYP phosphatase in their pathogenesis. PubMed: 35152348DOI: 10.1007/s00018-022-04173-w PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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