4xfn

</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=4xfn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xfn OCA], [https://pdbe.org/4xfn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xfn RCSB], [https://www.ebi.ac.uk/pdbsum/4xfn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xfn ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The tetrameric thyroxine transport protein transthyretin (TTR) forms amyloid fibrils upon dissociation and monomer unfolding. The aggregation of transthyretin has been reported as the cause of the life-threatening transthyretin amyloidosis. The standard treatment of familial cases of TTR amyloidosis has been liver transplantation. Although aggregation-preventing strategies involving ligands are known, understanding the mechanism of TTR aggregation can lead to additional inhibition approaches. Several models of TTR amyloid fibrils have been proposed, but the segments that drive aggregation of the protein have remained unknown. Here we identify beta-strands F and H as necessary for TTR aggregation. Based on the crystal structures of these segments, we designed two non-natural peptide inhibitors that block aggregation. This work provides the first characterization of peptide inhibitors for TTR aggregation, establishing a novel therapeutic strategy.

Uncovering the Mechanism of Aggregation of Human Transthyretin.,Saelices L, Johnson LM, Liang WY, Sawaya MR, Cascio D, Ruchala P, Whitelegge J, Jiang L, Riek R, Eisenberg DS J Biol Chem. 2015 Nov 27;290(48):28932-43. doi: 10.1074/jbc.M115.659912. Epub, 2015 Oct 12. PMID:26459562<ref>PMID:26459562</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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