Protein Variants | Comment | Organism |
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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 | UniProt | Comment | Textmining |
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Homo sapiens | - |
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- |