7cfz

From Proteopedia

(Difference between revisions)

Revision as of 07:37, 19 January 2022

SH3 domain of NADPH oxidase activator 1

Structural highlights

7cfz is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	NOXA1, P51NOX (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[NOXA1_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 PubMed

NADPH 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

↑ Geiszt M, Lekstrom K, Witta J, Leto TL. Proteins homologous to p47phox and p67phox support superoxide production by NAD(P)H oxidase 1 in colon epithelial cells. J Biol Chem. 2003 May 30;278(22):20006-12. Epub 2003 Mar 25. PMID:12657628 doi:http://dx.doi.org/10.1074/jbc.M301289200
↑ Takeya R, Ueno N, Kami K, Taura M, Kohjima M, Izaki T, Nunoi H, Sumimoto H. Novel human homologues of p47phox and p67phox participate in activation of superoxide-producing NADPH oxidases. J Biol Chem. 2003 Jul 4;278(27):25234-46. Epub 2003 Apr 25. PMID:12716910 doi:http://dx.doi.org/10.1074/jbc.M212856200
↑ Cheng G, Lambeth JD. NOXO1, regulation of lipid binding, localization, and activation of Nox1 by the Phox homology (PX) domain. J Biol Chem. 2004 Feb 6;279(6):4737-42. Epub 2003 Nov 14. PMID:14617635 doi:http://dx.doi.org/10.1074/jbc.M305968200
↑ Kawahara T, Kuwano Y, Teshima-Kondo S, Takeya R, Sumimoto H, Kishi K, Tsunawaki S, Hirayama T, Rokutan K. Role of nicotinamide adenine dinucleotide phosphate oxidase 1 in oxidative burst response to Toll-like receptor 5 signaling in large intestinal epithelial cells. J Immunol. 2004 Mar 1;172(5):3051-8. PMID:14978110
↑ Cheng G, Ritsick D, Lambeth JD. Nox3 regulation by NOXO1, p47phox, and p67phox. J Biol Chem. 2004 Aug 13;279(33):34250-5. Epub 2004 Jun 4. PMID:15181005 doi:http://dx.doi.org/10.1074/jbc.M400660200
↑ Ueno N, Takeya R, Miyano K, Kikuchi H, Sumimoto H. The NADPH oxidase Nox3 constitutively produces superoxide in a p22phox-dependent manner: its regulation by oxidase organizers and activators. J Biol Chem. 2005 Jun 17;280(24):23328-39. Epub 2005 Apr 11. PMID:15824103 doi:10.1074/jbc.M414548200
↑ Valente AJ, El Jamali A, Epperson TK, Gamez MJ, Pearson DW, Clark RA. NOX1 NADPH oxidase regulation by the NOXA1 SH3 domain. Free Radic Biol Med. 2007 Aug 1;43(3):384-96. Epub 2007 Apr 29. PMID:17602954 doi:http://dx.doi.org/S0891-5849(07)00289-4
↑ Gianni D, Diaz B, Taulet N, Fowler B, Courtneidge SA, Bokoch GM. Novel p47(phox)-related organizers regulate localized NADPH oxidase 1 (Nox1) activity. Sci Signal. 2009 Sep 15;2(88):ra54. doi: 10.1126/scisignal.2000370. PMID:19755710 doi:http://dx.doi.org/10.1126/scisignal.2000370
↑ Attri P, Park JH, De Backer J, Kim M, Yun JH, Heo Y, Dewilde S, Shiratani M, Choi EH, Lee W, Bogaerts A. Structural modification of NADPH oxidase activator (Noxa 1) by oxidative stress: An experimental and computational study. Int J Biol Macromol. 2020 Nov 15;163:2405-2414. doi:, 10.1016/j.ijbiomac.2020.09.120. Epub 2020 Sep 19. PMID:32961197 doi:http://dx.doi.org/10.1016/j.ijbiomac.2020.09.120

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7cfz"

@@ Line 1: / Line 1: @@
 ==SH3 domain of NADPH oxidase activator 1==
-<StructureSection load='7cfz' size='340' side='right'caption='[[7cfz]]' scene=''>
+<StructureSection load='7cfz' size='340' side='right'caption='[[7cfz]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CFZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CFZ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[7cfz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CFZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CFZ FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7cfz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cfz OCA], [https://pdbe.org/7cfz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cfz RCSB], [https://www.ebi.ac.uk/pdbsum/7cfz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cfz ProSAT]</span></td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NOXA1, P51NOX ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7cfz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cfz OCA], [https://pdbe.org/7cfz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cfz RCSB], [https://www.ebi.ac.uk/pdbsum/7cfz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cfz ProSAT]</span></td></tr>
 </table>
+== Function ==
+[[https://www.uniprot.org/uniprot/NOXA1_HUMAN NOXA1_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.<ref>PMID:12657628</ref> <ref>PMID:12716910</ref> <ref>PMID:14617635</ref> <ref>PMID:14978110</ref> <ref>PMID:15181005</ref> <ref>PMID:15824103</ref> <ref>PMID:17602954</ref> <ref>PMID:19755710</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+NADPH 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<ref>PMID:32961197</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 7cfz" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>
+[[Category: Human]]
 [[Category: Large Structures]]
-[[Category: Attri P]]
+[[Category: Attri, P]]
-[[Category: Kim M]]
+[[Category: Kim, M]]
-[[Category: Lee W]]
+[[Category: Lee, W]]
-[[Category: Park JH]]
+[[Category: Park, J H]]
+[[Category: Cytosolic protein]]
+[[Category: Nadph oxidase activator 1]]
+[[Category: Noxa1]]
+[[Category: Sh3]]

7cfz

From Proteopedia

Revision as of 07:37, 19 January 2022

SH3 domain of NADPH oxidase activator 1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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