End-binding protein

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 2: Line 2:
-
'''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<ref>PMID:11470413</ref>.
+
'''End-binding protein''' or '''telomere-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<ref>PMID:11470413</ref>.
</StructureSection>
</StructureSection>

Revision as of 09:20, 13 July 2021

Human end-binding protein 1 C terminal (grey) complex with dynactin-1 CAP-GLY domain (green) (PDB code 2hkq)

Drag the structure with the mouse to rotate

3D Structures of end-binding protein

Updated on 13-July-2021

References

  1. ↑ Nakamura M, Zhou XZ, Lu KP. Critical role for the EB1 and APC interaction in the regulation of microtubule polymerization. Curr Biol. 2001 Jul 10;11(13):1062-7. PMID:11470413

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel

Retrieved from "http://52.214.119.220/wiki/index.php/End-binding_protein"
Personal tools