3FTK

NVGSNTY segment from Islet Amyloid Polypeptide (IAPP or Amylin), hydrated crystal form

3FTK の概要

• エントリーDOI: 10.2210/pdb3ftk/pdb
• 関連するPDBエントリー: 3FOD 3FPO 3FQP 3FR1 3FTH 3FTK
• 分子名称: NVGSNTY heptapeptide segment from Islet Amyloid Polypeptide (2 entities in total)
• 機能のキーワード: amyloid-like protofibril, protein fibril
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 753.76

構造登録者

Wiltzius, J.J.W.,Sawaya, M.R.,Eisenberg, D. (登録日: 2009-01-13, 公開日: 2009-06-30, 最終更新日: 2024-02-21)

主引用文献

Wiltzius, J.J.,Landau, M.,Nelson, R.,Sawaya, M.R.,Apostol, M.I.,Goldschmidt, L.,Soriaga, A.B.,Cascio, D.,Rajashankar, K.,Eisenberg, D.
Molecular mechanisms for protein-encoded inheritance
Nat.Struct.Mol.Biol., 16:973-978, 2009

PubMed Abstract: In prion inheritance and transmission, strains are phenotypic variants encoded by protein 'conformations'. However, it is unclear how a protein conformation can be stable enough to endure transmission between cells or organisms. Here we describe new polymorphic crystal structures of segments of prion and other amyloid proteins, which offer two structural mechanisms for the encoding of prion strains. In packing polymorphism, prion strains are encoded by alternative packing arrangements (polymorphs) of beta-sheets formed by the same segment of a protein; in segmental polymorphism, prion strains are encoded by distinct beta-sheets built from different segments of a protein. Both forms of polymorphism can produce enduring conformations capable of encoding strains. These molecular mechanisms for transfer of protein-encoded information into prion strains share features with the familiar mechanism for transfer of nucleic acid-encoded information into microbial strains, including sequence specificity and recognition by noncovalent bonds.

PubMed: 19684598
DOI: 10.1038/nsmb.1643

実験手法

X-RAY DIFFRACTION (1.5 Å)