2RNM
Structure of The HET-s(218-289) prion in its amyloid form obtained by solid-state NMR
Summary for 2RNM
Entry DOI | 10.2210/pdb2rnm/pdb |
Descriptor | Small s protein (1 entity in total) |
Functional Keywords | het-s(218-289), beta-solenoid, prion, amyloid fibril, parallel beta-sheets, hydrophobic core, salt bridges, asparagine ladders, beta-helix, protein fibril |
Biological source | Podospora anserina (Fungi) |
Cellular location | Cytoplasm: Q03689 |
Total number of polymer chains | 5 |
Total formula weight | 43338.25 |
Authors | Wasmer, C.,Lange, A.,Van Melckebeke, H.,Siemer, A.,Riek, R.,Meier, B.H. (deposition date: 2008-01-24, release date: 2008-04-01, Last modification date: 2024-05-01) |
Primary citation | Wasmer, C.,Lange, A.,Van Melckebeke, H.,Siemer, A.B.,Riek, R.,Meier, B.H. Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core Science, 319:1523-1526, 2008 Cited by PubMed: 18339938DOI: 10.1126/science.1151839 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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