2. Academic Validation
  3. NMR structure and regulated expression in APL cell of human SH3BGRL3

NMR structure and regulated expression in APL cell of human SH3BGRL3

  • FEBS Lett. 2005 May 23;579(13):2788-94. doi: 10.1016/j.febslet.2005.04.011.
Chao Xu 1,  Peizheng Zheng,  Shuhong Shen,  Yingqi Xu,  Ling Wei,  Hengjun Gao,  Shengnian Wang,  Chongri Zhu,  Yajun Tang,  Jihui Wu,  Qinghua Zhang,  Yunyu Shi
Affiliations

Affiliation

  • 1 Hefei National Laboratory for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China.
PMID: 15907482 DOI: 10.1016/j.febslet.2005.04.011
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 alpha (TNF-alpha) 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.

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