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2RNM

Structure of The HET-s(218-289) prion in its amyloid form obtained by solid-state NMR

Summary for 2RNM
Entry DOI10.2210/pdb2rnm/pdb
DescriptorSmall s protein (1 entity in total)
Functional Keywordshet-s(218-289), beta-solenoid, prion, amyloid fibril, parallel beta-sheets, hydrophobic core, salt bridges, asparagine ladders, beta-helix, protein fibril
Biological sourcePodospora anserina (Fungi)
Cellular locationCytoplasm: Q03689
Total number of polymer chains5
Total formula weight43338.25
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: 2015-07-08)
Primary citationWasmer, 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: 18339938
DOI: 10.1126/science.1151839
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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