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Literature summary for 1.6.3.1 extracted from

  • Shen, K.; Sergeant, S.; Hantgan, R.R.; McPhail, L.C.; Horita, D.A.
    Mutations in the PX-SH3A linker of p47phox decouple PI(3,4)P2 binding from NADPH oxidase activation (2008), Biochemistry, 47, 8855-8865.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
additional information the linker region between the phox homology domain and N-terminal SH3 domain plays a role in blocking the binding of the phosphoinositide 3,4-bisphosphate. Replacement of linker residues 151-158 with glycine alters NMR-measured spin lattice relaxation rates and sedimentation velocity, suggesting that the phox homology domain is released from its autoinhibited conformation. The mutant displays phosphoinositide 3,4-bisphosphate binding activity comparable to that of the isolated phox homology domain but has greatly reduced NAD(P)H oxidase activity upon activation Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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