1ueg: Difference between revisions

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[[Image:1ueg.jpg|left|200px]]
[[Image:1ueg.jpg|left|200px]]


{{Structure
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|SITE=
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|GENE= EB1 (amino acids 1-130) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
{{STRUCTURE_1ueg| PDB=1ueg |  SCENE= }}  
|RELATEDENTRY=[[1pa7|1PA7]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ueg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ueg OCA], [http://www.ebi.ac.uk/pdbsum/1ueg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ueg RCSB]</span>
}}


'''Crystal structure of amino-terminal microtubule binding domain of EB1'''
'''Crystal structure of amino-terminal microtubule binding domain of EB1'''
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[[Category: Hayashi, I.]]
[[Category: Hayashi, I.]]
[[Category: Ikura, M.]]
[[Category: Ikura, M.]]
[[Category: ch domain]]
[[Category: Ch domain]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 11:06:29 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:09:12 2008''

Revision as of 11:06, 3 May 2008

File:1ueg.jpg

Template:STRUCTURE 1ueg

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 Page seeded by OCA on Sat May 3 11:06:29 2008

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