Expression And Circular Dichroism Structure Analysis Of The Protein Fragment Encoded By The Mutant Col4A5 Gene
Keywords
Nephritis, Hereditary/Genetics, Mutation, Collagen, Structure
Abstract
Purpose: By analyzing the protein structure after point mutation of col4a5 gene, explore the impact of gene mutation on the basic structure and possible secondary structure of the encoded protein. Methods: Diagnosed X-linked dominant hereditary alport syndrome (alport syndrome, as) The patient’s ¦Á5(¢¤) chain is the research object. The point mutation g.3246g>t in col4a5 causes one of the glycines in the encoded protein to be replaced by valine p.g1015v. The patient’s d5(¢¤) chain is expressed separately using e.coli. The domain containing the mutation site and the same domain of the control ¦Á5(¢¤) chain were tested by circular dichroism spectroscopy and the differences in their secondary structures were compared. Results: The wavelength of the lowest peak of the patient’s circular dichroism spectrum was about 200nm from the control. , changed to about 220nm, and the kurtosis decreased. Secondary structure analysis showed that the fusion protein from the control was mainly ¦Â-sheet and random coil, without ¦Á-helical structure, while about 1% of the fusion protein from the patient appeared /8 ¦Á-helical structure. Conclusion: When a glycine in the collagen region is replaced by valine during as, it not only changes the local secondary structure where the substitution occurs, but also changes the folding dynamics of the entire ¦Á5(¢¤) chain. Change. Abnormally folded peptide chains will affect the interactions between chains, or prevent the normal formation of triple helix molecules, or make the formed triple helix molecules loose in structure and easily destroyed by protease degradation, eventually causing the glomerular basement membrane to appear characteristic pathological changes.
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Original research was done by Wang Yunfeng, Ding Jie, Bu Dingfang, Wang Fang
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