1SJ6

NMR Structure and Regulated Expression in APL Cell of Human SH3BGRL3

1SJ6 の概要

• エントリーDOI: 10.2210/pdb1sj6/pdb
• NMR情報: BMRB: 6152
• 分子名称: SH3 domain-binding glutamic acid-rich-like protein 3 (1 entity in total)
• 機能のキーワード: thioredoxin, nuclear protein, protein binding
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q9H299
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11518.83

構造登録者

Xu, C.,Tang, Y.,Xu, Y.,Wu, J.,Shi, Y.,Zhang, Q.,Zheng, P.,Du, Y. (登録日: 2004-03-03, 公開日: 2005-03-22, 最終更新日: 2024-05-29)

主引用文献

Xu, C.,Zheng, P.,Shen, S.,Xu, Y.,Wei, L.,Gao, H.,Wang, S.,Zhu, C.,Tang, Y.,Wu, J.,Zhang, Q.,Shi, Y.
NMR structure and regulated expression in APL cell of human SH3BGRL3.
Febs Lett., 579:2788-2794, 2005

PubMed 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.

PubMed: 15907482
DOI: 10.1016/j.febslet.2005.04.011

実験手法

SOLUTION NMR