[HTML][HTML] Crystal structure of the amino-terminal microtubule-binding domain of end-binding protein 1 (EB1)
I Hayashi, M Ikura - Journal of Biological Chemistry, 2003 - ASBMB
The end-binding protein 1 (EB1) family is a highly conserved group of proteins that localizes
to the plus-ends of microtubules. EB1 has been shown to play an important role in regulating
microtubule dynamics and chromosome segregation, but its regulation mechanism is poorly
understood. We have determined the 1.45-Å resolution crystal structure of the amino-
terminal domain of EB1, which is essential for microtubule binding, and show that it forms a
calponin homology (CH) domain fold that is found in many proteins involved in the actin …
to the plus-ends of microtubules. EB1 has been shown to play an important role in regulating
microtubule dynamics and chromosome segregation, but its regulation mechanism is poorly
understood. We have determined the 1.45-Å resolution crystal structure of the amino-
terminal domain of EB1, which is essential for microtubule binding, and show that it forms a
calponin homology (CH) domain fold that is found in many proteins involved in the actin …