Biology:PX domain

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1h6h.png
PX domain of NADH oxidase (p40phox), lipid-bound
Identifiers
SymbolPX
PfamPF00787
InterProIPR001683
SMARTPX
PROSITEPDOC50195
SCOP21h6h / SCOPe / SUPFAM
OPM superfamily57
OPM protein1xte
CDDcd06093

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.

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. PMID 8931154. 
  2. "Phoxy lipids: revealing PX domains as phosphoinositide binding modules". Cell 105 (7): 817–20. June 2001. doi:10.1016/S0092-8674(01)00414-7. PMID 11439176. 
  3. "Solution structure of the PX domain, a target of the SH3 domain". Nat. Struct. Biol. 8 (6): 526–30. June 2001. doi:10.1038/88591. PMID 11373621. 
  4. "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. October 2002. doi:10.1093/emboj/cdf519. PMID 12356722. 
  5. "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. April 2003. doi:10.1073/pnas.0735712100. PMID 12672956. Bibcode2003PNAS..100.4474A.