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Title | Structure of Dimeric and Tetrameric Complexes of the BAR Domain Protein PICK1 Determined by Small-Angle X-Ray Scattering. |
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Journal, issue, pages | Structure, Vol. 23, Issue 7, Page 1258-1270, Year 2015 |
Publish date | Jul 7, 2015 |
![]() | Morten L Karlsen / Thor S Thorsen / Niklaus Johner / Ina Ammendrup-Johnsen / Simon Erlendsson / Xinsheng Tian / Jens B Simonsen / Rasmus Høiberg-Nielsen / Nikolaj M Christensen / George Khelashvili / Werner Streicher / Kaare Teilum / Bente Vestergaard / Harel Weinstein / Ulrik Gether / Lise Arleth / Kenneth L Madsen / ![]() ![]() |
PubMed Abstract | PICK1 is a neuronal scaffolding protein containing a PDZ domain and an auto-inhibited BAR domain. BAR domains are membrane-sculpting protein modules generating membrane curvature and promoting ...PICK1 is a neuronal scaffolding protein containing a PDZ domain and an auto-inhibited BAR domain. BAR domains are membrane-sculpting protein modules generating membrane curvature and promoting membrane fission. Previous data suggest that BAR domains are organized in lattice-like arrangements when stabilizing membranes but little is known about structural organization of BAR domains in solution. Through a small-angle X-ray scattering (SAXS) analysis, we determine the structure of dimeric and tetrameric complexes of PICK1 in solution. SAXS and biochemical data reveal a strong propensity of PICK1 to form higher-order structures, and SAXS analysis suggests an offset, parallel mode of BAR-BAR oligomerization. Furthermore, unlike accessory domains in other BAR domain proteins, the positioning of the PDZ domains is flexible, enabling PICK1 to perform long-range, dynamic scaffolding of membrane-associated proteins. Together with functional data, these structural findings are compatible with a model in which oligomerization governs auto-inhibition of BAR domain function. |
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Methods | SAS (X-ray synchrotron) |
Structure data | ![]() SASDAB8: |
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