7n8r
From Proteopedia
(Difference between revisions)
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==FGTGFG segment from the Nucleoporin p54, residues 63-68== | ==FGTGFG segment from the Nucleoporin p54, residues 63-68== | ||
| - | <StructureSection load='7n8r' size='340' side='right'caption='[[7n8r]]' scene=''> | + | <StructureSection load='7n8r' size='340' side='right'caption='[[7n8r]], [[Resolution|resolution]] 1.20Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7N8R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7N8R FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7n8r]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7N8R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7N8R FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7n8r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7n8r OCA], [https://pdbe.org/7n8r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7n8r RCSB], [https://www.ebi.ac.uk/pdbsum/7n8r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7n8r ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TFA:TRIFLUOROACETIC+ACID'>TFA</scene></td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7n8r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7n8r OCA], [https://pdbe.org/7n8r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7n8r RCSB], [https://www.ebi.ac.uk/pdbsum/7n8r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7n8r ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The assembly of proteins into fibrillar amyloid structures was once considered to be pathologic and essentially irreversible. Recent studies reveal amyloid-like structures that form reversibly, derived from protein low-complexity domains which function in cellular metabolism. Here, by comparing atomic-level structures of reversible and irreversible amyloid fibrils, we find that the beta-sheets of reversible fibrils are enriched in flattened (as opposed to pleated) beta-sheets formed by stacking of extended beta-strands. Quantum mechanical calculations show that glycine residues favor extended beta-strands which may be stabilized by intraresidue interactions between the amide proton and the carbonyl oxygen, known as C5 hydrogen-bonds. Larger residue side chains favor shorter strands and pleated sheets. These findings highlight a structural element that may regulate reversible amyloid assembly. | ||
| + | |||
| + | Extended beta-Strands Contribute to Reversible Amyloid Formation.,Murray KA, Evans D, Hughes MP, Sawaya MR, Hu CJ, Houk KN, Eisenberg D ACS Nano. 2022 Feb 8. doi: 10.1021/acsnano.1c08043. PMID:35132852<ref>PMID:35132852</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7n8r" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Eisenberg | + | [[Category: Eisenberg, D S]] |
| - | [[Category: Hughes | + | [[Category: Hughes, M P]] |
| - | [[Category: Sawaya | + | [[Category: Sawaya, M R]] |
| + | [[Category: Amyloid-like fibril]] | ||
| + | [[Category: Protein fibril]] | ||
Revision as of 07:21, 9 March 2022
FGTGFG segment from the Nucleoporin p54, residues 63-68
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