2rnm
From Proteopedia
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| - | + | ==Structure of The HET-s(218-289) prion in its amyloid form obtained by solid-state NMR== | |
| - | + | <StructureSection load='2rnm' size='340' side='right' caption='[[2rnm]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2rnm]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Podospora_anserina Podospora anserina]. The May 2008 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Prions'' by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2008_5 10.2210/rcsb_pdb/mom_2008_5]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RNM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RNM FirstGlance]. <br> | |
| + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2rnm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rnm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rnm RCSB], [http://www.ebi.ac.uk/pdbsum/2rnm PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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<ref>PMID:18339938</ref> | |
| - | + | ||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
==See Also== | ==See Also== | ||
| - | *[[Human Prion Protein Dimer|Human Prion Protein Dimer]] | ||
*[[Prion|Prion]] | *[[Prion|Prion]] | ||
*[[Prion protein|Prion protein]] | *[[Prion protein|Prion protein]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Podospora anserina]] | [[Category: Podospora anserina]] | ||
[[Category: Prions]] | [[Category: Prions]] | ||
[[Category: RCSB PDB Molecule of the Month]] | [[Category: RCSB PDB Molecule of the Month]] | ||
| - | [[Category: Lange, A | + | [[Category: Lange, A]] |
| - | [[Category: Meier, B H | + | [[Category: Meier, B H]] |
| - | [[Category: Melckebeke, H Van | + | [[Category: Melckebeke, H Van]] |
| - | [[Category: Riek, R | + | [[Category: Riek, R]] |
| - | [[Category: Siemer, A | + | [[Category: Siemer, A]] |
| - | [[Category: Wasmer, C | + | [[Category: Wasmer, C]] |
[[Category: Amyloid fibril]] | [[Category: Amyloid fibril]] | ||
[[Category: Asparagine ladder]] | [[Category: Asparagine ladder]] | ||
Revision as of 14:12, 17 December 2014
Structure of The HET-s(218-289) prion in its amyloid form obtained by solid-state NMR
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