Paxillin

spinqualitylabelsall models Human paxillin LD4 domain complex (sky blue) withα-parvin (green), tetraethylene glycol, triethylene glycol and etylene glycol (PDB code 2vzi) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Paxillin (PXN) is involved in actin membrane attachment at sites of cell adhesion to focal adhesion domains. PXN contains a number of domains which are involved in protein-protein interactions: LD, LIM, SH2 and SH3 binding sites. LD motifs are leucine-rich sequences which begin with leucine (L) and end with aspartate (D). PXN serves as a docking protein recruiting signaling molecules to focal adhesions. Disease PXN has enhanced expression in several types of cancer. PXN mutations are associated with lung cancer tumor growth. Structural highlights PXN LD motifs are localized on the N-terminal region while the LIM double zinc finger domains are found at the C-terminal. Human paxillin LD4 domain interactions with α-parvin.

3D structures of paxillin

Updated on 24-August-2017

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• Paxillin LD1 domain
  • 4edn – hPXN + beta-parvin CH2 domain - human
    
  • 2k2r – hPXN + beta-parvin CH2 domain - NMR
    
  • 2vzg, 2vzd – hPXN + alpha-parvin C terminal
    
  • 3rqe – hPXN + CCM3
    
• Paxillin LD2 domain
  • 4xgz – hPXN + antibody
    
  • 3u3f – hPXN + tyrosine kinase PYK2 focal adhesion domain
    
  • 1ow8 – hPXN + focal adhesion kinase focal adhesion targeting domain
    
  • 3rqf – hPXN + CCM3
    
• Paxillin LD4 domain
  • 4r32 – cPXN + tyrosine kinase PYK2 focal adhesion targeting domain - chicken
    
  • 1ow6, 3gm1 – hPXN + tyrosine kinase PYK2 focal adhesion targeting domain
    
  • 1ow7 – hPXN + focal adhesion kinase focal adhesion targeting domain
    
  • 2l6f – hPXN + focal adhesion kinase focal adhesion targeting domain - NMR
    
  • 4xh2 – hPXN + antibody
    
  • 2vzi – hPXN + alpha-parvin C terminal
    
  • 3rqg – hPXN + CCM3
    
• Paxillin proline-rich region
  • 2o9v – hPXN + ponsin SH3 domain
    

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