We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
NMR structure and regulated expression in APL cell of human SH3BGRL3
- Authors
Xu, Chao; Zheng, Peizheng; Shen, Shuhong; Xu, Yingqi; Wei, Ling; Gao, Hengjun; Wang, Shengnian; Zhu, Chongri; Tang, Yajun; Wu, Jihui; Zhang, Qinghua; Shi, Yunyu
- Abstract
Abstract: SH3 domain binding glutamic acid-rich protein like 3 (SH3BGRL3) is the new member of thioredoxin (TRX) super family, whose posttranslational modified form was identified as tumor necrosis factor α (TNF-α) inhibitory protein, TIP-B1. In this paper, we determined its solution structure by multi-dimensional nuclear magnetic resonance spectroscopy. The overall structure of human SH3BGRL3 conformed to a TRX-like fold. To understand its function in vivo, the upregulated expression in acute promyelocytic leukemia cell line NB4 at both mRNA and protein level was elucidated. Immunofluorescence and immunohistochemistry staining with monoclonal antibody against SH3BGRL3 demonstrated that it was a cytoplasmic protein in both NB4 cell and human tissues. These results, as a whole, indicate that SH3BGRL3 may function as a regulator in all-trans retinoic acid-induced pathway.
- Subjects
NUCLEAR magnetic resonance; GLUTAMIC acid; TRETINOIN; RESONANCE
- Publication
FEBS Letters, 2005, Vol 579, Issue 13, p2788
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2005.04.011