1UEG

Crystal structure of amino-terminal microtubule binding domain of EB1

Summary for 1UEG

• Entry DOI: 10.2210/pdb1ueg/pdb
• Related: 1PA7
• Descriptor: Microtubule-associated protein RP/EB family member 1, SULFATE ION (3 entities in total)
• Functional Keywords: ch domain, structural protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytoskeleton: Q15691
• Total number of polymer chains: 1
• Total formula weight: 15146.45

Authors

Hayashi, I.,Ikura, M. (deposition date: 2003-05-14, release date: 2003-10-21, Last modification date: 2023-12-27)

Primary citation

Hayashi, I.,Ikura, M.
Crystal structure of the amino-terminal microtubule-binding domain of end-binding protein 1 (EB1)
J.Biol.Chem., 278:36430-36434, 2003

PubMed Abstract: 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-A 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 cytoskeleton. The functional CH domain for actin binding is a tandem pair, whereas EB1 is the first example of a single CH domain that can associate with the microtubule filament. Although our biochemical study shows that microtubule binding of EB1 is electrostatic in part, our mutational analysis suggests that the hydrophobic network, which is partially exposed in our crystal structure, is also important for the association. We propose that, like other actin-binding CH domains, EB1 employs the hydrophobic interaction to bind to microtubules.

PubMed: 12857735
DOI: 10.1074/jbc.M305773200

Experimental method

X-RAY DIFFRACTION (2.4 Å)