2rnm: Difference between revisions

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[[Image:2rnm.~~jpg~~|left|200px]]

[[Image:2rnm.png|left|200px]]

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~~==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 [http://en.wikipedia.org/wiki/Podospora_anserina Podospora anserina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RNM 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:[http://www.ncbi.nlm.nih.gov/pubmed/18339938 18339938]

[[Category: Podospora anserina]]

[[Category: Single protein]]

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[[Category: Protein fibril]]

[[Category: Salt bridge]]

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-[[Image:2rnm.jpg|left|200px]]
+[[Image:2rnm.png|left|200px]]
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-==Overview==
+{{ABSTRACT_18339938}}
-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==
 RNM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Podospora_anserina Podospora anserina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RNM 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:[http://www.ncbi.nlm.nih.gov/pubmed/18339938 18339938]
 [[Category: Podospora anserina]]
 [[Category: Single protein]]
@@ Line 37: / Line 33: @@
 [[Category: Protein fibril]]
 [[Category: Salt bridge]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 17:13:32 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 26 18:22:37 2008''