Journal article
Crystallization and preliminary X-ray analysis of the N-terminal domain of human thioredoxin-interacting protein
G Polekhina, DB Ascher, SF Kok, M Waltham
Acta Crystallographica Section F Structural Biology and Crystallization Communications | INT UNION CRYSTALLOGRAPHY | Published : 2011
Abstract
Thioredoxin-interacting protein (TXNIP) is a negative regulator of thioredoxin and its roles in the pathologies of diabetes and cardiovascular diseases have marked it out as a potential drug target. Expression of TXNIP is robustly induced under various stress conditions such as high glucose, heat shock, UV, H2O2 and mechanical stress amongst others. Elevated levels of TXNIP result in the sequestration and inactivation of thioredoxin, leading to cellular oxidative stress. For some time, this was the only known function of TXNIP; however, more recently the protein has been shown to play a role in regulation of glucose uptake and activation of the inflammasome. Based on the primary sequence, TX..
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Funding Acknowledgements
GP is a recipient of a Career Development Award from the National Health and Medical Research Council (NHMRC) of Australia. This work was also supported by a grant from NHMRC to GP and MW. DBA was an Australian Postgraduate Award Scholar and a recipient of a St Vincent's Institute Foundation Scholarship sponsored by Colin North and Major Engineering. This research was undertaken at the Australian Synchrotron, Victoria, Australia. We appreciate the support provided by all staff at the Australian synchrotron during our visits. We would also like to acknowledge the staff and particularly Dr Janet Newman at the Bio21 Collaborative Crystallographic Centre at CSIRO Molecular and Health Technologies, Parkville, Melbourne.