6c3s | pdb_00006c3s

AMYLOID FORMING PEPTIDE YTIAAL FROM TRANSTHYRETIN

spinqualitylabelsall models 6c3s, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6c3s is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 6c3f, 6c3g Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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