3QH9
Human Liprin-beta2 Coiled-Coil
Summary for 3QH9
| Entry DOI | 10.2210/pdb3qh9/pdb |
| Descriptor | Liprin-beta-2, IODIDE ION, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | coiled-coil, dimerization, structural protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 9979.14 |
| Authors | Stafford, R.L.,Tang, M.,Phillips, M.L.,Bowie, J.U. (deposition date: 2011-01-25, release date: 2011-10-26, Last modification date: 2024-02-21) |
| Primary citation | Stafford, R.L.,Tang, M.Y.,Sawaya, M.R.,Phillips, M.L.,Bowie, J.U. Crystal structure of the central coiled-coil domain from human liprin-beta2 Biochemistry, 50:3807-3815, 2011 Cited by PubMed Abstract: Liprins are a conserved family of scaffolding proteins important for the proper regulation and development of neuronal synapses. Humans have four liprin-αs and two liprin-βs which all contain long coiled-coil domains followed by three tandem SAM domains. Complex interactions between the coiled-coil and SAM domains are thought to create liprin scaffolds, but the structural and biochemical properties of these domains remain largely uncharacterized. In this study we find that the human liprin-β2 coiled-coil forms an extended dimer. Several protease-resistant subdomains within the liprin-β1 and liprin-β2 coiled-coils were also identified. A 2.0 Å crystal structure of the central, protease-resistant core of the liprin-β2 coiled-coil reveals a parallel helix orientation. These studies represent an initial step toward determining the overall architecture of liprin scaffolds and understanding the molecular basis for their synaptic functions. PubMed: 21462929DOI: 10.1021/bi200141e PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.01 Å) |
Structure validation
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