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6C3T

AMYLOID FORMING PEPTIDE AADTWE FROM TRANSTHYRETIN WITH ATTR-D38A MUTATION ASSOCIATED WITH A FAMILIAL FORM OF TRANSTHYRETIN AMYLOIDOSIS

6C3T の概要
エントリーDOI10.2210/pdb6c3t/pdb
関連するPDBエントリー6C3F 6C3G 6C3S
分子名称ALA-ALA-ASP-THR-TRP-GLU (2 entities in total)
機能のキーワードamyloid, transthyretin, fibril, protein fibril
由来する生物種Homo sapiens
タンパク質・核酸の鎖数2
化学式量合計1383.37
構造登録者
Sievers, S.A.,Sawaya, M.R.,Saelices, L.,Eisenberg, D.S. (登録日: 2018-01-10, 公開日: 2018-04-18, 最終更新日: 2024-04-03)
主引用文献Saelices, L.,Sievers, S.A.,Sawaya, M.R.,Eisenberg, D.S.
Crystal structures of amyloidogenic segments of human transthyretin.
Protein Sci., 27:1295-1303, 2018
Cited by
PubMed Abstract: 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 β-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.
PubMed: 29626847
DOI: 10.1002/pro.3420
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1 Å)
構造検証レポート
Validation report summary of 6c3t
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-01-15に公開中

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