文章基本信息

标题：Taxon-specific zeta-crystallin of camel eye lens: A comparative in silico studies
本地全文：下载
作者：Ajamaluddin Malik ; Javed Masood Khan ; Malik Hisamuddin 等
期刊名称：Journal of King Saud University - Science
印刷版ISSN：1018-3647
出版年度：2022
卷号：34
期号：4
页码：1-8
DOI：10.1016/j.jksus.2022.101973
语种：English
出版社：Elsevier
摘要：AbstractThe eye lens is a specialized organ of the visual system, which is transparent due to its complex geometry and unique protein composition. Nature has designed it to focus light on the retina throughout the life span. Several factors (post-translational modifications, thermal and solar radiations) causes aggregation of the lens proteins and result in early-onset of cataract. A cataract is one of the major causes of blindness worldwide. It's interesting how camel eyes maintain lens transparency in a harsh desert climate? The camel eye lenses contain a novel protein zeta (ζ)-crystallin in a bulk amount that is also present in two other animals (guinea pig and Japanese frog) but is adopted for milder habitats. The camel lens ζ-crystallin is a poorly characterized protein. This study has investigated the physicochemical and structural properties of camel, guinea pig, and Japanese frog’s ζ-crystallin. The docking results showed a strong affinity between NADPH and ζ-crystallin. RMSD, RMSF, radius of gyration, and SASA analysis in the ligand-free and bound states showed distinct prope6rties in these ζ-crystallins. Moreover, the hydrophobicity of camel and Japanese frog ζ-crystallin is lower than ζ-crystallin of other mammalian sources. The unique physicochemical and structural properties of taxon-specific ζ-crystallin are likely to maintain lens transparency.
关键词：KeywordsenZeta-crystallinStructure modelingEye lens proteinsCamelProtein solubility