2X3X
structure of mouse syndapin I (crystal form 1)
Summary for 2X3X
| Entry DOI | 10.2210/pdb2x3x/pdb |
| Related | 2X3V 2X3W |
| Descriptor | PROTEIN KINASE C AND CASEIN KINASE SUBSTRATE IN NEURONS PROTEIN 1 (2 entities in total) |
| Functional Keywords | endocytosis, phosphoprotein, bar, n-wasp, dynamin, pacsin i, transferase |
| Biological source | MUS MUSCULUS (HOUSE MOUSE) More |
| Cellular location | Cytoplasm (By similarity): Q61644 Q61644 |
| Total number of polymer chains | 5 |
| Total formula weight | 131510.94 |
| Authors | Ma, Q.,Rao, Y.,Vahedi-Faridi, A.,Saenger, W.,Haucke, V. (deposition date: 2010-01-28, release date: 2010-04-07, Last modification date: 2024-05-08) |
| Primary citation | Rao, Y.,Ma, Q.,Vahedi-Faridi, A.,Sundborger, A.,Pechstein, A.,Puchkov, D.,Luo, L.,Shupliakov, O.,Saenger, W.,Haucke, V. Molecular Basis for SH3 Domain Regulation of F-Bar-Mediated Membrane Deformation. Proc.Natl.Acad.Sci.USA, 107:8213-, 2010 Cited by PubMed Abstract: Members of the Bin/amphiphysin/Rvs (BAR) domain protein superfamily are involved in membrane remodeling in various cellular pathways ranging from endocytic vesicle and T-tubule formation to cell migration and neuromorphogenesis. Membrane curvature induction and stabilization are encoded within the BAR or Fer-CIP4 homology-BAR (F-BAR) domains, alpha-helical coiled coils that dimerize into membrane-binding modules. BAR/F-BAR domain proteins often contain an SH3 domain, which recruits binding partners such as the oligomeric membrane-fissioning GTPase dynamin. How precisely BAR/F-BAR domain-mediated membrane deformation is regulated at the cellular level is unknown. Here we present the crystal structures of full-length syndapin 1 and its F-BAR domain. Our data show that syndapin 1 F-BAR-mediated membrane deformation is subject to autoinhibition by its SH3 domain. Release from the clamped conformation is driven by association of syndapin 1 SH3 with the proline-rich domain of dynamin 1, thereby unlocking its potent membrane-bending activity. We hypothesize that this mechanism might be commonly used to regulate BAR/F-BAR domain-induced membrane deformation and to potentially couple this process to dynamin-mediated fission. Our data thus suggest a structure-based model for SH3-mediated regulation of BAR/F-BAR domain function. PubMed: 20404169DOI: 10.1073/PNAS.1003478107 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.35 Å) |
Structure validation
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