1XTN,2V6V,1KMD,1OCU,2RAK,2I4K,1O7K,2ETT,2AR5,1H6H,2V14


Conserved Protein Domain Family
PX_domain

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cd06093: PX_domain 
Click on image for an interactive view with Cn3D
The Phox Homology domain, a phosphoinositide binding module
The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting.
Statistics
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PSSM-Id: 132768
View PSSM: cd06093
Aligned: 206 rows
Threshold Bit Score: 31.5591
Threshold Setting Gi: 68846537
Created: 25-Apr-2007
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
 
phosphoinosit..
Conserved site includes 6 residues -Click on image for an interactive view with Cn3D
Feature 1:phosphoinositide binding site [chemical binding site]
Evidence:
  • Comment:A majority of PX domain containing proteins binds phosphatidylinositol-3-phosphate (PI3P) at this site. In some cases, other phosphoinositides, such as PI4P or PI(3,4)P2, are the preferred substrates.
  • Structure:1H6H_A; Human P40(phox) PX domain binds Phosphatidylinositol 3-Phosphate; defined at 3.5A contacts.
    View structure with Cn3D
  • Structure:1OCU_A; Saccharomyces cerevisiae SNX3 PX domain binds Phosphatidylinositol-3-Phosphate; defined at 3.5A contacts.
    View structure with Cn3D
  • 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                                                      ###                             ## 
1XTN_A          9 SVSIPSSDehre------kkkRFTVYKVLVSvgr----seWFVFRRYAEFDKLYNSLKKqfp-------amALKIPAKRi 71
gi 212542911  912 SLFVEDATvrfilksgaqassDTTSVNGTTYa-------iTTCRRSFADFEHLAKCLAVehp------asyIPSISEARs 978
gi 50288053   138 IINIEPIEngge------sgiDNIQFKIILHsgl---ttkSTVIRKLSDFYVLYRQLQSnnwgviipppplLCQLPDKVk 208
gi 2507154    107 TLLAKVTGlerfgsatgkkenPTIIFDCSTNlptfrkqqyKNVKKSYEEFHQLFKYLNVaiq------esfVPTLPSAYt 180
gi 50553400   695 YCEILRSVia----------dGELCFVIKTRqdg----klSAVRRPYSDFVFLQKWLAHeqp------lswFPALMTPTn 754
gi 71031190     7 SVSVKKGKs------------HRFQYEINIAynd----wsWSRYRTFAEFEELQRDLEQnf--------cdVPSLPDIEf 62
gi 118362139  923 DLKVVSFEqsek------fdkRTVVFNISFFdsk---gesMIIQRSYREFNDLYKYLSSkyr------qykFANFPKKQn 987
gi 145536490   77 TSTVVGYEkvqkg----ifmsTYVYFKIETKpi------nWVVRRTYEEFIALKNMLNKhy---------nVPNIPNQRk 137
gi 209877018    7 DVNVFDYYks----------gHSVVFKIKITdinr--kesWYISKSYKEFVQVDDFFRLr-----------YPSIPELPy 63
gi 159119804  581 YVRYLDYRkvfdr----fthtQVLMFIFAVSsqe---rklKCISKTYEDFHVLHKELVGafg------ysaVPGLPSFRs 647
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
Feature 1                        #                             
1XTN_A         72 fgdn---fdpdFIKQRRAGLNEFIQNLVRYpelynhpdVRAFLQM 113
gi 212542911  979 pfqihskpsraILHDMQGRLDQFLRILLTHptfathemLWEFFLM 1023
gi 50288053   209 p---------sITDTCRNQMQMMLEHILNNeylrndidFKCFLNS 244
gi 2507154    181 tfgi---nseeDRMKVTRNFQLWFNRLSQDpliirneeVAFFIES 222
gi 50553400   755 pfaiphrpsreILHAMHLRLNLFLRTLLLHptfsnhelLWEWLLV 799
gi 71031190    63 aagl---galeHLHNAVDYLDTFLKELFNRpdtrcsqhLLEFVDL 104
gi 118362139  988 kaq----lssqELVDRTNQFNIYLQSVVTLikee-vnvINHFLSK 1027
gi 145536490  138 sp------vefTYIKQLRHLQMFLNFVLLDqeirslpvIQDFLSL 176
gi 209877018   64 egwww-qhndqFYKYQLEELQAYMDSILKNdpgienmvLKYFLDL 107
gi 159119804  648 mnmg--ggrheVIHDTQKRLTKYLTEINNVqalrtsaiYRSFLKH 690

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