Login / Signup

Crystal Structure of Cocosin, A Potential Food Allergen from Coconut (Cocos nucifera).

Teng-Chuan JinCheng WangCaiying ZhangYang WangYu-Wei ChenFeng GuoAndrew HowardMin-Jie CaoTong-Jen FuTara H McHughYu-Zhu Zhang
Published in: Journal of agricultural and food chemistry (2017)
Coconut (Cocos nucifera) is an important palm tree. Coconut fruit is widely consumed. The most abundant storage protein in coconut fruit is cocosin (a likely food allergen), which belongs to the 11S globulin family. Cocosin was crystallized near a century ago, but its structure remains unknown. By optimizing crystallization conditions and cryoprotectant solutions, we were able to obtain cocosin crystals that diffracted to 1.85 Å. The cocosin gene was cloned from genomic DNA isolated from dry coconut tissue. The protein sequence deduced from the predicted cocosin coding sequence was used to guide model building and structure refinement. The structure of cocosin was determined for the first time, and it revealed a typical 11S globulin feature of a double layer doughnut-shaped hexamer.
Keyphrases
  • amino acid
  • human health
  • copy number
  • gene expression
  • risk assessment
  • genome wide
  • single molecule
  • binding protein
  • allergic rhinitis
  • cell free
  • small molecule
  • dna methylation
  • room temperature
  • ionic liquid