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Human and Tree Shrew Alpha-synuclein: Comparative cDNA Sequence and Protein Structure Analysis.

Zheng-Cun Wu1,2, Zhang-Qiong Huang1,2, Qin-Fang Jiang1,2

  • 1Institute of Medical Biology, Chinese Academy of Medical Sciences and Peking Union Medical College, Kunming, 650118, China.

Applied Biochemistry and Biotechnology
|August 13, 2015
PubMed
Summary

Tree shrew alpha-synuclein (α-syn) shares high similarity with human α-syn, suggesting its potential as a model for neurodegenerative diseases. This research details the tree shrew α-syn sequence and structure.

Keywords:
Alpha-synucleinProtein structureTree shrewcDNA

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Genetics

Background:

  • Alpha-synuclein (α-syn) is implicated in neurodegenerative diseases.
  • Understanding α-syn in diverse species aids in disease research.
  • Limited data exists on tree shrew α-syn cDNA and protein structure.

Purpose of the Study:

  • To determine the cDNA sequence and predict the protein structure of tree shrew α-syn.
  • To analyze the homology between tree shrew and human α-syn.
  • To evaluate the potential of tree shrews as an animal model for α-synucleinopathies.

Main Methods:

  • Designed primers based on human α-syn cDNA.
  • Obtained and sequenced tree shrew α-syn cDNA using RT-PCR.
  • Predicted and analyzed amino acid sequence and spatial structure.

Main Results:

  • Tree shrew α-syn cDNA sequence shows high homology to human sequence, with specific nucleotide differences.
  • Tree shrew α-syn protein sequence is 97.1% identical to human α-syn.
  • Secondary and spatial structures of tree shrew α-syn are identical to human α-syn; phosphorylation sites are conserved except at position 103.

Conclusions:

  • Alpha-synuclein likely functions similarly in tree shrews and humans.
  • Tree shrew α-syn exhibits high structural and sequence conservation with human α-syn.
  • Tree shrews represent a promising animal model for studying α-synucleinopathies.