5H0X

Crystal structure of H88S mutated human transthyretin

5H0X の概要

• エントリーDOI: 10.2210/pdb5h0x/pdb
• 関連するPDBエントリー: 5H0V 5H0W 5H0Y 5H0Z
• 分子名称: Transthyretin (2 entities in total)
• 機能のキーワード: transthhyretin, amyloidosis, transporter, transport protein
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Secreted: P02766
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 27851.06

構造登録者

Yokoyama, T.,Hanawa, Y.,Obita, T.,Mizuguchi, M. (登録日: 2016-10-07, 公開日: 2017-06-14, 最終更新日: 2024-03-20)

主引用文献

Yokoyama, T.,Hanawa, Y.,Obita, T.,Mizuguchi, M.
Stability and crystal structures of His88 mutant human transthyretins
FEBS Lett., 591:1862-1871, 2017

PubMed Abstract: Destabilization of human transthyretin (TTR) has been implicated in its misfolding and aggregation. A previous study on the neutron crystal structure of TTR suggested that a large hydrogen bond network around H88 which includes water molecules is significantly involved in the stability of wild-type TTR (WT-TTR). Here, we demonstrate that the H88R mutant associated with amyloid cardiomyopathy is substantially destabilized compared with WT-TTR. In order to clarify the role of H88 and the hydrogen bond network in the stability of TTR, we determined the thermodynamic stability and the crystal structure of H88 mutants (H88A, H88F, H88Y, and H88S). Our results suggest that in some cases TTR is destabilized due to alterations in bound water molecules as well as structural changes in TTR itself.

PubMed: 28563699
DOI: 10.1002/1873-3468.12704

実験手法

X-RAY DIFFRACTION (1.573 Å)