1ueg: Difference between revisions
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'''Crystal structure of amino-terminal microtubule binding domain of EB1''' | {{Structure | ||
|PDB= 1ueg |SIZE=350|CAPTION= <scene name='initialview01'>1ueg</scene>, resolution 2.40Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= | |||
|GENE= EB1 (amino acids 1-130) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''Crystal structure of amino-terminal microtubule binding domain of EB1''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1UEG is a [ | 1UEG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UEG OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12857735 12857735] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ch domain]] | [[Category: ch domain]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:30:57 2008'' | ||
Revision as of 15:30, 20 March 2008
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| , resolution 2.40Å | |||||||
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| Ligands: | |||||||
| Gene: | EB1 (amino acids 1-130) (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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