1SJ6

NMR Structure and Regulated Expression in APL Cell of Human SH3BGRL3

Summary for 1SJ6

• Entry DOI: 10.2210/pdb1sj6/pdb
• NMR Information: BMRB: 6152
• Descriptor: SH3 domain-binding glutamic acid-rich-like protein 3 (1 entity in total)
• Functional Keywords: thioredoxin, nuclear protein, protein binding
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q9H299
• Total number of polymer chains: 1
• Total formula weight: 11518.83

Authors

Xu, C.,Tang, Y.,Xu, Y.,Wu, J.,Shi, Y.,Zhang, Q.,Zheng, P.,Du, Y. (deposition date: 2004-03-03, release date: 2005-03-22, Last modification date: 2024-05-29)

Primary citation

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

Experimental method

SOLUTION NMR