End-binding protein

spinqualitylabelsall models Human end-binding protein 1 C terminal (grey) complex with dynactin-1 CAP-GLY domain (green) (PDB code 2hkq) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Updated on 26-July-2015 {{#tree:id=OrganizedByTopic|openlevels=0|' scene=> End-binding protein (EB) regulates microtubules dynamics, promotes colony formation and enhances tumor growth. EB is part of the proteins which accumulate at the growing microtubule plus end. During mitosis the EB associates with centrosome and spindle microtubules. EB is involved in the regulation of chromosome stability and microtubule structure. The C terminal domains of EB1 and EB3 are involved in dimer formation. The CH (Calponin Homology) domain is an actin-binding domain.

3D Structures of end-binding protein

Updated on 26-July-2015

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• End-binding protein 1 (MAPRE1)

• • 1pa7, 1ueg, 1vka, 2r8u – hEB1 N terminal – human
    
  • 1wu9 – hEB1 C terminal
    
  • 1yib, 1yig – hEB1 C terminal (mutant)
    
  • 1txq, 2hkq, 2hl5 – hEB1 C terminal + dynactin
    
  • 3gjo – hEB1 C terminal + dystonin
    
  • 2qjz – hEB1 CH domain
    
  • 1v5k – EB1 CH domain (mutant) – mouse - NMR
    
• End-binding protein 3

• • 3co1 – hEB3 CH domain
    
  • 1wyo – hEB3 CH domain - NMR
    
• End-binding protein 1+3

• • 3tq7 – hEB3 C terminal + hEB1 C terminal + dynactin
    

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Michal Harel, Openfox