7n8r: Difference between revisions

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'''Unreleased structure'''


The entry 7n8r is ON HOLD  until Paper Publication
==FGTGFG segment from the Nucleoporin p54, residues 63-68==
<StructureSection load='7n8r' size='340' side='right'caption='[[7n8r]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7n8r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2&#8491;</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>
== Function ==
[https://www.uniprot.org/uniprot/NUP54_HUMAN NUP54_HUMAN] Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane.
<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.


Authors: Hughes, M.P., Sawaya, M.R., Eisenberg, D.S.
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>


Description: FGTGFG segment from the Nucleoporin p54, residues 63-68
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Eisenberg, D.S]]
<div class="pdbe-citations 7n8r" style="background-color:#fffaf0;"></div>
[[Category: Sawaya, M.R]]
== References ==
[[Category: Hughes, M.P]]
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Eisenberg DS]]
[[Category: Hughes MP]]
[[Category: Sawaya MR]]
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