Article
ATP differentially antagonizes the crowding-induced destabilization of human γS-crystallin and its four cataract-causing mutants.
Biochemical and biophysical research communications - 17 Dec 2020
He Yuan, Kang Jian, Song Jianxing
Abstract excerpt
αβγ-crystallins account for ∼90% of ocular proteins in lens with concentrations ≥400 mg/ml, which has to be soluble for the whole life-span and their aggregation results in cataract. So far, four cataract-causing mutants G18V, D26G, S39C and V42 M have been identified for human γS-crystallin. Mysteriously, lens maintains ATP concentrations of 3-7 mM despite being a metabolically-quiescent organ. Here by DSF and...
Topics
Join the communities discussing this publication.