1ueg
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Crystal structure of amino-terminal microtubule binding domain of EB1
OverviewOverview
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.
About this StructureAbout this Structure
1UEG is a Single protein structure of sequence from Homo sapiens with SO4 as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the amino-terminal microtubule-binding domain of end-binding protein 1 (EB1)., Hayashi I, Ikura M, J Biol Chem. 2003 Sep 19;278(38):36430-4. Epub 2003 Jul 11. PMID:12857735
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