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In silico studies to explain the interactions to inactivate NAPDH oxidase by apocynin and its dimmer
Author(s) -
Macías-Pérez Martha Edith,
Martínez-Ramos Federico,
Padilla-Martínez Itzia Irene,
Correa-Basurto José,
Tolentino-López Luis Esteban,
Rosales-Hernández Martha Cecilia
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.962.4
Subject(s) - apocynin , p22phox , nadph oxidase , chemistry , superoxide , oxidase test , protein subunit , in silico , protein data bank (rcsb pdb) , nitric oxide , biochemistry , biophysics , enzyme , biology , organic chemistry , gene
NADPH oxidase has been considered a therapeutic target in hypertension disease due to superoxide anion (O2•‐) react with Nitric Oxide (NO) diminish its vasodilator effect. Apocynin dimer has been reported as NADPH oxidase inhibitor due to that is able to interact with the p47phox subunit and prevent the binding with the p22phox subunit, however this fact has been not reported for apocynin. For this reason a in silico study was done to know the interactions between apocynin and its dimmer with two different conformations of p47phox one in extended conformation (1NG2.pdb), and the other in close conformation (1WLP.pdb) which consist of: two SH3 domains and a polybasic region, that are important during the coupling with the p22phox subunit. The results showed that in the extend conformation apocynin is bind at the SH3B domain of p47phox meanwhile its dimmer is bind at the polybasic region maintained to p47phox in its autoinhibited form avoiding the coupling with p22phox. Groemping Y., Lapouge K., Smerdon S.J., Rittinger K. Molecular Basis of Phosphorylatión‐induced Activatión of the NADPH oxidase. Cell. 2003;343–355.