- Protein Classification
- Protein Links
 | lumenal side |
| cytoplasmic side |
| 1h6h » PX domain of NADH oxidase (p40phox), ligand-bound | |
|---|---|
| Depth | 3.9 ± 2.0 Å |
| Tilt Angle | 55 ± 14° |
| ΔGtransfer | -6.0 kcal/mol |
| Links to 1h6h | PDB Sum, PDB, SCOP, MSD, OCA, MMDB |
| Topology | cytoplasmic |
| Resolution | 1.70 Å |
| Other PDB entries representing this structure | 2dyb |
| Number of subunits | 1 |
| Experimental Verification for 1h6h » PX domain of NADH oxidase (p40phox), ligand-bound |
|---|
| Residues embedded in the hydrophobic interior of the membrane are F35, Y94 and V95. This is consistent with the important role of F35, Y94 and V95 in interactions with lipid bilayers (Stahelin et al. 2003). This orientation was calculated including atoms of the bound ligand (inositol lipid). Orientation of apo-protein is slightly different (V97 of apo-protein also penetrates the membrane core). Maximal membrane binding affinity is -12.6 kcal/mol (Stahelin et al. 2003), which is higher than calculated transfer energy of the apo-protein (-4.5 kcal/mol) due to strong specific binding of phosphoinositide. |
| 2 references |
|---|
| Cho W, Stahelin RV. 2005. Membrane-protein interactions in cell signaling and membrane trafficking. Annu Rev Biophys Biomol Struct. 34:119-51. PubMed |
| Stahelin, R.V., Burian, A., Bruzik, K.S., Murray, D., and Cho, W. 2003. Membrane binding mechanisms of the PX domains of NADPH oxidase p40phox and p47phox. J. Biol. Chem. 278:14469-14479. PubMed |
| Comments on 1h6h » PX domain of NADH oxidase (p40phox), ligand-bound |
|---|
| Subcellular localization of PX domains - see Cho and Stahelin (2005). |
