The PX domain is a phosphoinositide-binding structural domain involved in targeting of proteins to cell membranes.
 PX domain of NADH oxidase (p40phox), lipid-bound | |||||||||
| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Symbol | PX | ||||||||
| Pfam | PF00787 | ||||||||
| InterPro | IPR001683 | ||||||||
| SMART | PX | ||||||||
| PROSITE | PDOC50195 | ||||||||
| SCOP2 | 1h6h / SCOPe / SUPFAM | ||||||||
| OPM superfamily | 57 | ||||||||
| OPM protein | 1xte | ||||||||
| CDD | cd06093 | ||||||||
| |||||||||
This domain was first found in P40phox and p47phox domains of NADPH oxidase (phox stands for phagocytic oxidase).[1][2] It was also identified in many other proteins involved in membrane trafficking, including nexins, Phospholipase D, and phosphoinositide-3-kinases.
The PX domain is structurally conserved in eukaryotes, although amino acid sequences show little similarity.[3] PX domains interact primarily with PtdIns(3)P lipids.[4][5] However some of them bind to phosphatidic acid, PtdIns(3,4)P2, PtdIns(3,5)P2, PtdIns(4,5)P2, and PtdIns(3,4,5)P3. The PX-domain can also interact with other domains and proteins.
Human proteins containing this domain
editSorting nexins contain this domain. Other examples include:
References
edit- ^ Ponting CP (November 1996). "Novel domains in NADPH oxidase subunits, sorting nexins, and PtdIns 3-kinases: binding partners of SH3 domains?". Protein Sci. 5 (11): 2353–7. doi:10.1002/pro.5560051122. PMC 2143296. PMID 8931154.2353-7&rft.date=1996-11&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2143296#id-name=PMC&rft_id=info:pmid/8931154&rft_id=info:doi/10.1002/pro.5560051122&rft.au=Ponting CP&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2143296&rfr_id=info:sid/en.wikipedia.org:PX domain" class="Z3988">
- ^ Wishart MJ, Taylor GS, Dixon JE (June 2001). "Phoxy lipids: revealing PX domains as phosphoinositide binding modules". Cell. 105 (7): 817–20. doi:10.1016/S0092-8674(01)00414-7. PMID 11439176. S2CID 12622490.817-20&rft.date=2001-06&rft_id=https://api.semanticscholar.org/CorpusID:12622490#id-name=S2CID&rft_id=info:pmid/11439176&rft_id=info:doi/10.1016/S0092-8674(01)00414-7&rft.aulast=Wishart&rft.aufirst=MJ&rft.au=Taylor, GS&rft.au=Dixon, JE&rft_id=https://doi.org/10.1016%2FS0092-8674%2801%2900414-7&rfr_id=info:sid/en.wikipedia.org:PX domain" class="Z3988">
- ^ Hiroaki H, Ago T, Ito T, Sumimoto H, Kohda D (June 2001). "Solution structure of the PX domain, a target of the SH3 domain". Nat. Struct. Biol. 8 (6): 526–30. doi:10.1038/88591. PMID 11373621. S2CID 27416988.526-30&rft.date=2001-06&rft_id=https://api.semanticscholar.org/CorpusID:27416988#id-name=S2CID&rft_id=info:pmid/11373621&rft_id=info:doi/10.1038/88591&rft.aulast=Hiroaki&rft.aufirst=H&rft.au=Ago, T&rft.au=Ito, T&rft.au=Sumimoto, H&rft.au=Kohda, D&rfr_id=info:sid/en.wikipedia.org:PX domain" class="Z3988">
- ^ Karathanassis D, Stahelin RV, Bravo J, Perisic O, Pacold CM, Cho W, Williams RL (October 2002). "Binding of the PX domain of p47phox to phosphatidylinositol 3,4-bisphosphate and phosphatidic acid is masked by an intramolecular interaction". EMBO J. 21 (19): 5057–68. doi:10.1093/emboj/cdf519. PMC 129041. PMID 12356722.5057-68&rft.date=2002-10&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC129041#id-name=PMC&rft_id=info:pmid/12356722&rft_id=info:doi/10.1093/emboj/cdf519&rft.aulast=Karathanassis&rft.aufirst=D&rft.au=Stahelin, RV&rft.au=Bravo, J&rft.au=Perisic, O&rft.au=Pacold, CM&rft.au=Cho, W&rft.au=Williams, RL&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC129041&rfr_id=info:sid/en.wikipedia.org:PX domain" class="Z3988">
- ^ Ago T, Kuribayashi F, Hiroaki H, Takeya R, Ito T, Kohda D, Sumimoto H (April 2003). "Phosphorylation of p47phox directs phox homology domain from SH3 domain toward phosphoinositides, leading to phagocyte NADPH oxidase activation". Proc. Natl. Acad. Sci. U.S.A. 100 (8): 4474–9. Bibcode:2003PNAS..100.4474A. doi:10.1073/pnas.0735712100. PMC 153580. PMID 12672956.4474-9&rft.date=2003-04&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC153580#id-name=PMC&rft_id=info:pmid/12672956&rft_id=info:doi/10.1073/pnas.0735712100&rft_id=info:bibcode/2003PNAS..100.4474A&rft.aulast=Ago&rft.aufirst=T&rft.au=Kuribayashi, F&rft.au=Hiroaki, H&rft.au=Takeya, R&rft.au=Ito, T&rft.au=Kohda, D&rft.au=Sumimoto, H&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC153580&rfr_id=info:sid/en.wikipedia.org:PX domain" class="Z3988">