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From Proteopedia
SH3 domain of NADPH oxidase activator 1
Structural highlights
FunctionNOXA1_HUMAN Functions as an activator of NOX1, a superoxide-producing NADPH oxidase. Functions in the production of reactive oxygen species (ROS) which participate in a variety of biological processes including host defense, hormone biosynthesis, oxygen sensing and signal transduction. May also activate CYBB/gp91phox and NOX3.[1] [2] [3] [4] [5] [6] [7] [8] Publication Abstract from PubMedNADPH oxidases 1 (NOX1) derived reactive oxygen species (ROS) play an important role in the progression of cancer through signaling pathways. Therefore, in this paper, we demonstrate the effect of cold atmospheric plasma (CAP) on the structural changes of Noxa1 SH3 protein, one of the regulatory subunits of NOX1. For this purpose, firstly we purified the Noxa1 SH3 protein and analyzed the structure using X-ray crystallography, and subsequently, we treated the protein with two types of CAP reactors such as pulsed dielectric barrier discharge (DBD) and Soft Jet for different time intervals. The structural deformation of Noxa1 SH3 protein was analyzed by various experimental methods (circular dichroism, fluorescence, and NMR spectroscopy) and by MD simulations. Additionally, we demonstrate the effect of CAP (DBD and Soft Jet) on the viability and expression of NOX1 in A375 cancer cells. Our results are useful to understand the structural modification/oxidation occur in protein due to reactive oxygen and nitrogen (RONS) species generated by CAP. Structural modification of NADPH oxidase activator (Noxa 1) by oxidative stress: An experimental and computational study.,Attri P, Park JH, De Backer J, Kim M, Yun JH, Heo Y, Dewilde S, Shiratani M, Choi EH, Lee W, Bogaerts A Int J Biol Macromol. 2020 Nov 15;163:2405-2414. doi:, 10.1016/j.ijbiomac.2020.09.120. Epub 2020 Sep 19. PMID:32961197[9] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Homo sapiens | Large Structures | Attri P | Kim M | Lee W | Park JH
