2rnm
From Proteopedia
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'''Structure of The HET-s(218-289) prion in its amyloid form obtained by solid-state NMR''' | '''Structure of The HET-s(218-289) prion in its amyloid form obtained by solid-state NMR''' | ||
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[[Category: Siemer, A.]] | [[Category: Siemer, A.]] | ||
[[Category: Wasmer, C.]] | [[Category: Wasmer, C.]] | ||
| - | [[Category: | + | [[Category: Amyloid fibril]] |
| - | [[Category: | + | [[Category: Asparagine ladder]] |
| - | [[Category: | + | [[Category: Beta-helix]] |
| - | [[Category: | + | [[Category: Beta-solenoid]] |
| - | [[Category: | + | [[Category: Hydrophobic core]] |
| - | + | [[Category: Parallel beta-sheet]] | |
| - | [[Category: | + | [[Category: Prion]] |
| - | [[Category: | + | [[Category: Protein fibril]] |
| - | [[Category: | + | [[Category: Salt bridge]] |
| - | [[Category: | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:13:32 2008'' |
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Revision as of 14:13, 4 May 2008
Structure of The HET-s(218-289) prion in its amyloid form obtained by solid-state NMR
Overview
Prion and nonprion forms of proteins are believed to differ solely in their three-dimensional structure, which is therefore of paramount importance for the prion function. However, no atomic-resolution structure of the fibrillar state that is likely infectious has been reported to date. We present a structural model based on solid-state nuclear magnetic resonance restraints for amyloid fibrils from the prion-forming domain (residues 218 to 289) of the HET-s protein from the filamentous fungus Podospora anserina. On the basis of 134 intra- and intermolecular experimental distance restraints, we find that HET-s(218-289) forms a left-handed beta solenoid, with each molecule forming two helical windings, a compact hydrophobic core, at least 23 hydrogen bonds, three salt bridges, and two asparagine ladders. The structure is likely to have broad implications for understanding the infectious amyloid state.
About this Structure
2RNM is a Single protein structure of sequence from Podospora anserina. Full crystallographic information is available from OCA.
Reference
Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core., Wasmer C, Lange A, Van Melckebeke H, Siemer AB, Riek R, Meier BH, Science. 2008 Mar 14;319(5869):1523-6. PMID:18339938 Page seeded by OCA on Sun May 4 17:13:32 2008
