2ktm
From Proteopedia
(Difference between revisions)
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<StructureSection load='2ktm' size='340' side='right' caption='[[2ktm]], [[NMR_Ensembles_of_Models | 12 NMR models]]' scene=''> | <StructureSection load='2ktm' size='340' side='right' caption='[[2ktm]], [[NMR_Ensembles_of_Models | 12 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2ktm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2ktm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ovis_ammon_aries Ovis ammon aries]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KTM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KTM FirstGlance]. <br> |
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1y2s|1y2s]], [[1tpx|1tpx]], [[1xyu|1xyu]], [[1tqb|1tqb]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1y2s|1y2s]], [[1tpx|1tpx]], [[1xyu|1xyu]], [[1tqb|1tqb]]</td></tr> | ||
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PRNP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9940 Ovis aries])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PRNP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9940 Ovis ammon aries])</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=2ktm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ktm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ktm RCSB], [http://www.ebi.ac.uk/pdbsum/2ktm PDBsum]</span></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=2ktm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ktm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ktm RCSB], [http://www.ebi.ac.uk/pdbsum/2ktm PDBsum]</span></td></tr> | ||
</table> | </table> | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Aggregation and misfolding of the prion protein (PrP) are thought to be the cause of a family of lethal neurodegenerative diseases affecting humans and other animals. Although the structures of PrP from several species have been solved, still little is known about the mechanisms that lead to the misfolded species. Here, we show that the region of PrP comprising the hairpin formed by the helices H2 and H3 is a stable independently folded unit able to retain its secondary and tertiary structure also in the absence of the rest of the sequence. We also prove that the isolated H2H3 is highly fibrillogenic and forms amyloid fibers morphologically similar to those obtained for the full-length protein. Fibrillization of H2H3 but not of full-length PrP is concomitant with formation of aggregates. These observations suggest a "banana-peeling" mechanism for misfolding of PrP in which H2H3 is the aggregation seed that needs to be first exposed to promote conversion from a helical to a beta-rich structure. | ||
| + | |||
| + | Prion fibrillization is mediated by a native structural element that comprises helices H2 and H3.,Adrover M, Pauwels K, Prigent S, de Chiara C, Xu Z, Chapuis C, Pastore A, Rezaei H J Biol Chem. 2010 Jul 2;285(27):21004-12. doi: 10.1074/jbc.M110.111815. Epub 2010, Apr 7. PMID:20375014<ref>PMID:20375014</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
==See Also== | ==See Also== | ||
*[[Prion|Prion]] | *[[Prion|Prion]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Ovis aries]] | + | [[Category: Ovis ammon aries]] |
[[Category: Adrover, M]] | [[Category: Adrover, M]] | ||
[[Category: Chiara, C de]] | [[Category: Chiara, C de]] | ||
Revision as of 12:02, 18 March 2015
Solution NMR structure of H2H3 domain of ovine prion protein (residues 167-234)
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