Cataract-causing mutation S228P promotes βB1-crystallin aggregation and degradation by separating two interacting loops in C-terminal domain

Cataract-causing mutation S228P promotes βB1-crystallin aggregation and degradation by separating two interacting loops in C-terminal domain

Abstract β/γ-Crystallins are predominant structural proteins in the cytoplasm of lens fiber cells and share a similar fold composing of four Greek-key motifs divided into two domains. Numerous cataract-causing mutations have been identified in various β/γ-crystallins, but the mechanisms underlying c...

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Bibliographic Details
Main Authors: Liang-Bo Qi, Li-Dan Hu, Huihui Liu, Hai-Yun Li, Xiao-Yao Leng, Yong-Bin Yan
Format: Article
Language:English
Published: SpringerOpen 2016-06-01
Series:Protein & Cell
Subjects:
β/γ-crystallin
cataract-causing mutation
hydrophobic core
protein aggregation
protein folding
Online Access:http://link.springer.com/article/10.1007/s13238-016-0284-3

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http://link.springer.com/article/10.1007/s13238-016-0284-3

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