PX domain

Last updated
1h6h.png
PX domain of NADH oxidase (p40phox), lipid-bound
Identifiers
SymbolPX
Pfam PF00787
InterPro IPR001683
SMART PX
PROSITE PDOC50195
SCOP2 1h6h / SCOPe / SUPFAM
OPM superfamily 57
OPM protein 1xte
CDD cd06093
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

The PX domain is a phosphoinositide-binding structural domain involved in targeting of proteins to cell membranes.

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. [6]

Human proteins containing this domain

The human genome encodes about 40 PX-domain proteins, [7] including multiple sorting nexins. Other examples include:

References

  1. ↑ 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.
  2. ↑ 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.
  3. ↑ 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.
  4. ↑ 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.
  5. ↑ 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.
  6. ↑ Vollert, Carolina S.; Uetz, Peter (November 2004). "The Phox Homology (PX) Domain Protein Interaction Network in Yeast". Molecular & Cellular Proteomics. 3 (11): 1053–1064. doi: 10.1074/mcp.M400081-MCP200 . PMID   15263065.
  7. ↑ Simonsen, A.; Stenmark, H. (August 2001). "PX domains: attracted by phosphoinositides". Nature Cell Biology. 3 (8): E179–182. doi:10.1038/35087112. ISSN   1465-7392. PMID   11483972.
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