1O7K,1KQ6,1GD5


Conserved Protein Domain Family
PX_p47phox

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cd06887: PX_p47phox 
Click on image for an interactive view with Cn3D
The phosphoinositide binding Phox Homology domain of the p47phox subunit of NADPH oxidase
The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. p47phox is a cytosolic subunit of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox), which plays a key role in the ability of phagocytes to defend against bacterial infections. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p47phox is required for activation of NADH oxidase and plays a role in translocation. It contains an N-terminal PX domain, two Src Homology 3 (SH3) domains, and a C-terminal domain that contains PxxP motifs for binding SH3 domains. The PX domain of p47phox is unique in that it contains two distinct basic pockets on the membrane-binding surface: one preferentially binds phosphatidylinositol-3,4-bisphosphate [PI(3,4)P2] and is analogous to the PI3P-binding pocket of p40phox, while the other binds anionic phospholipids such as phosphatidic acid or phosphatidylserine. Simultaneous binding in the two pockets results in increased membrane affinity. The PX domain of p47phox is also involved in protein-protein interaction.
Statistics
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PSSM-Id: 132797
View PSSM: cd06887
Aligned: 7 rows
Threshold Bit Score: 207.38
Threshold Setting Gi: 219454625
Created: 11-Jul-2008
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
 
phosphoinosit..anionic
Conserved site includes 6 residues -Click on image for an interactive view with Cn3D
Feature 1:phosphoinositide binding site [chemical binding site]
Evidence:
  • Structure:1O7K_A; Human P47(phox) PX domain binds a sulfate at the phosphoinositide binding site; defined at 4A contacts.
    View structure with Cn3D
  • Comment:P47(phox) binds phosphatidylinositol-3,4-bisphosphate at this site.
  • Comment:also based on the structures of phosphatidylinositol-3-phosphate bound to other members of this superfamily
  • Comment:Two basic residues are key in binding with phosphoinositides: one forms hydrogen bonds with the 3-phosphate of PI(3)P and another forms hydrogen bonds with the 4-and 5-hydroxyl groups of PI(3)P.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                              ###                               ##       
1O7K_A         14 IRHIALLGFEKRFVPSQHYVYXFLVKWQDLSEKVVYRRFTEIYEFHKTLKEXFPIEAGainPENRIIPHLPAPKWFDgq- 92
1KQ6_A          6 IRHIALLGFEKRFVPSQHYVYXFLVKWQDLSEKVVYRRFTEIYEFHKTLKEXFPIEAGainPENRIIPHLPAPKWFDgq- 84
1GD5_A          8 IRHIALLGFEKRFVPSQHYVYMFLVKWQDLSEKVVYRRFTEIYEFHKTLKEMFPIEAGainPENRIIPHLPAPKWFDgq- 86
gi 163914941    6 IRHIQLLGFEKRFIPSQHYVYMFMVKWQDLTEKLVYRKFTEIYEFHKSLKEMFPIEAGdisKEHRTIPHLPAPKWFDgl- 84
gi 71897087     6 IRHIELLGYEKRFFPSQHYVYMFLVKWNDLSEKLIYRRFTDIYEFHKALKEMFPIESGdinAENRIIPHLPAPKWFDgq- 84
gi 71834304     6 VRHVELLGFEKRFFPSQHYVYMLLVKWSDQSEKLVYRRYPEVHTLHKTLKEMFPIEAGdidEKDRIIPTLPAPKWLDnq- 84
gi 219454625  803 IAGVRLLGIEKRYVPNKHYLYILSVKWSEGSEFIIYRRYSAFFQLHEKLTELFPIETGvvsKKDQKIPALPKQRWFGnek 882
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
Feature 1               #                                 
1O7K_A         93 -rAAENRQGTLTEYCSTLXSLPtKISRCPHLLDFFKVRPD 131
1KQ6_A         85 -rAAENRQGTLTEYCSTLXSLPtKISRCPHLLDFFKVRPD 123
1GD5_A         87 -rAAENRQGTLTEYCSTLMSLPtKISRCPHLLDFFKVRPD 125
gi 163914941   85 -rSTENRQVTLSDYFSSLLSLPpKISRCPHVLNFFQVRSD 123
gi 71897087    85 -rSTQSRQGTLAEYCYTLVNLPhKISRCRHVVSFFEVRPD 123
gi 71834304    85 -kTTETRQATLAEYCRSLLNLPaNISRCQLIRDFFKMRPE 123
gi 219454625  883 fkVAERRQTTIDEYCRKVAMAEpKISEHEEVLSFFKTLPV 922

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