PX domain

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
SymbolPX
PfamPF00787
InterProIPR001683
SMARTPX
PROSITEPDOC50195
SCOP21h6h / SCOPe / SUPFAM
OPM superfamily57
OPM protein1xte
CDDcd06093
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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

Sorting nexins contain this domain. 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.
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