7P53

Crystal Structure of Human gamma-D-crystallin mutant C110M at 1.57 Angstroms resolution

7P53 の概要

• エントリーDOI: 10.2210/pdb7p53/pdb
• 分子名称: Gamma-crystallin D (2 entities in total)
• 機能のキーワード: cysteine mutation, recombinant, structural protein, eye lens
• 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: 20663.02

構造登録者

Strofaldi, A.,Khan, A.R.,McManus, J. (登録日: 2021-07-14, 公開日: 2021-10-13, 最終更新日: 2024-01-31)

主引用文献

Strofaldi, A.,Khan, A.R.,McManus, J.J.
Surface Exposed Free Cysteine Suppresses Crystallization of Human gamma D-Crystallin.
J.Mol.Biol., 433:167252-167252, 2021

PubMed Abstract: Human γD-crystallin (HGD) has remarkable stability against condensation in the human lens, sometimes over a whole lifetime. The native protein has a surface exposed free cysteine that forms dimers (Benedek, 1997; Ramkumar et al., 1864) without specific biological function and leads to further protein association and/or aggregation, which creates a paradox for understanding its stability. Previous work has demonstrated that chemical modification of the protein at the free cysteine (C110), increases the temperature at which liquid-liquid phase separation occurs (LLPS), lowers protein solubility and suggests an important role for this amino acid in maintaining its long-term resistance to condensation. Here we demonstrate that mutation of the cysteine does not alter the structure or solubility (liquidus) line for the protein, but dramatically increases the protein crystal nucleation rate following LLPS, suggesting that the free cysteine has a vital role in suppressing crystallization in the human lens.

PubMed: 34537240
DOI: 10.1016/j.jmb.2021.167252

実験手法

X-RAY DIFFRACTION (1.57 Å)