期刊
PROTEIN SCIENCE
卷 14, 期 10, 页码 2601-2609出版社
WILEY
DOI: 10.1110/ps.051579205
关键词
LEA; LEA14; NMR spectroscopy; structural genomics; fibronectin Type III fold
资金
- NCRR NIH HHS [P41 RR02301, P41 RR002301] Funding Source: Medline
- NIGMS NIH HHS [P50 GM64598, P41 GM66326, P41 GM066326, P50 GM064598] Funding Source: Medline
We report the three-dimensional structure of a late embryogenesis abundant (LEA) protein from Arabidopsis thaliana gene At1g01470.1. This protein is a member of Pfam cluster PF03168, and has been classified as a LEA14 protein. LEA proteins are expressed under conditions of cellular stress, such as desiccation, cold, osmotic stress, and heat. The structure, which was determined by NMR spectroscopy, revealed that the At1g01470.1 protein has an alpha beta-fold consisting of one alpha-helix and seven beta-strands that form two antiparallel beta-sheets. The closest structural homologs were discovered to be fibronectin Type III domains, which have < 7% sequence identity. Because fibronectins from animal cells have been shown to be involved in cell adhesion, cell motility, wound heating, and maintenance of cell shape, it is interesting to note that in plants wounding or stress results in the overexpression of a protein with fibronectin Type III structural features.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据