6c3f: Difference between revisions

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<StructureSection load='6c3f' size='340' side='right'caption='[[6c3f]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='6c3f' size='340' side='right'caption='[[6c3f]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6c3f]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C3F OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6C3F FirstGlance]. <br>
<table><tr><td colspan='2'>[[6c3f]] 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=6C3F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6C3F FirstGlance]. <br>
</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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.499&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6c3f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c3f OCA], [http://pdbe.org/6c3f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6c3f RCSB], [http://www.ebi.ac.uk/pdbsum/6c3f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6c3f ProSAT]</span></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=6c3f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c3f OCA], [https://pdbe.org/6c3f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6c3f RCSB], [https://www.ebi.ac.uk/pdbsum/6c3f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6c3f ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Amyloid diseases are characterized by the deposition of proteins in the form of amyloid fibrils, in organs that eventually fail. The development of effective drug candidates follows from the understanding of the molecular processes that lead to protein aggregation. Here we study amyloidogenic segments of transthyretin (TTR). TTR is a transporter of thyroxine and retinol in the blood and cerebrospinal fluid. When mutated and/or as a result of aging, TTR aggregates into amyloid fibrils that accumulate in organs such as the heart. Recently we reported two amyloidogenic segments that drive amyloid aggregation. Here we report the crystal structure of another six amyloidogenic segments of TTR. We found that the segments from the C-terminal region of TTR form in-register steric-zippers with highly-interdigitated, wet interfaces, whereas the beta-strand B from the N-terminal region of TTR forms an out-of-register assembly, previously associated with oligomeric formation. Our results contribute fundamental information for understanding the mechanism of aggregation of TTR. This article is protected by copyright. All rights reserved.
Crystal Structures of Amyloidogenic Segments of Human Transthyretin.,Saelices L, Sievers SA, Sawaya MR, Eisenberg DS Protein Sci. 2018 Apr 7. doi: 10.1002/pro.3420. PMID:29626847<ref>PMID:29626847</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6c3f" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Transthyretin 3D structures|Transthyretin 3D structures]]
*[[Transthyretin 3D structures|Transthyretin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Eisenberg, D S]]
[[Category: Eisenberg DS]]
[[Category: Saelices, L]]
[[Category: Saelices L]]
[[Category: Sawaya, M R]]
[[Category: Sawaya MR]]
[[Category: Amyloid]]
[[Category: Fibril]]
[[Category: Protein fibril]]
[[Category: Transthyretin]]
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