NMR structure of a major lens protein, Human ?C-Crystallin: Role of dipole moment in protein solubility.
 

NMR structure of a major lens protein, Human ?C-Crystallin: Role of dipole moment in protein solubility.

Related Articles NMR structure of a major lens protein, Human ?C-Crystallin: Role of dipole moment in protein solubility.

Biochemistry. 2016 May 17;

Authors: Dixit K, Pande A, Pande J, Sarma SP

Abstract
A hallmark of the crystallin proteins is their exceptionally high solubility, which is vital for maintaining the high refractive index of the eye lens. Human ?C-crystallin is a major ?-crystallin whose mutant forms are associated with congenital cataracts, but whose 3D-structure is not known. An earlier study on a homology model concluded that human ?C-crystallin has low intrinsic solubility, mainly due to the atypical magnitude and fluctuations of its dipole moment. Contrarily, the high-resolution tertiary structure of human ?C-crystallin determined here shows unequivocally that it is a highly soluble, monomeric molecule in solution. Notable differences between the orientations and interactions of several side chains are observed when compared to those in the model. No evidence for the pivotal role ascribed to the effect of dipole moment on protein solubility was found. The NMR structure should facilitate a comprehensive understanding of the deleterious effects of cataract-associated mutations in human ?C-crystallin.


PMID: 27187112 [PubMed - as supplied by publisher]



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