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[[Image:1wu9.gif|left|200px]]


{{Structure
==Crystal structure of the C-terminal domain of the end-binding protein 1 (EB1)==
|PDB= 1wu9 |SIZE=350|CAPTION= <scene name='initialview01'>1wu9</scene>, resolution 1.54&Aring;
<StructureSection load='1wu9' size='340' side='right'caption='[[1wu9]], [[Resolution|resolution]] 1.54&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1wu9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WU9 FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.54&#8491;</td></tr>
|GENE= EB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wu9 OCA], [https://pdbe.org/1wu9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wu9 RCSB], [https://www.ebi.ac.uk/pdbsum/1wu9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wu9 ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wu9 OCA], [http://www.ebi.ac.uk/pdbsum/1wu9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wu9 RCSB]</span>
[https://www.uniprot.org/uniprot/MARE1_HUMAN MARE1_HUMAN] Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes cytoplasmic microtubule nucleation and elongation. May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes. May play a role in cell migration.<ref>PMID:12388762</ref> <ref>PMID:21646404</ref> <ref>PMID:16109370</ref> <ref>PMID:19632184</ref>
}}
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wu/1wu9_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1wu9 ConSurf].
<div style="clear:both"></div>


'''Crystal structure of the C-terminal domain of the end-binding protein 1 (EB1)'''
==See Also==
 
*[[End-binding protein|End-binding protein]]
 
*[[Microtubule-associated protein 3D structures|Microtubule-associated protein 3D structures]]
==Overview==
== References ==
EB1 proteins bind to microtubule ends where they act in concert with other components, including the adenomatous polyposis coli (APC) tumor suppressor, to regulate the microtubule filament system. We find that EB1 is a stable dimer with a parallel coiled coil and show that dimerization is essential for the formation of its C-terminal domain (EB1-C). The crystal structure of EB1-C reveals a highly conserved surface patch with a deep hydrophobic cavity at its center. EB1-C binds two copies of an APC-derived C-terminal peptide (C-APCp1) with equal 5 microM affinity. The conserved APC Ile2805-Pro2806 sequence motif serves as an anchor for the interaction of C-APCp1 with the hydrophobic cavity of EB1-C. Phosphorylation of the conserved Cdc2 site Ser2789-Lys2792 in C-APCp1 reduces binding four-fold, indicating that the interaction APC-EB1 is post-translationally regulated in cells. Our findings provide a basis for understanding the dynamic crosstalk of EB1 proteins with their molecular targets in eukaryotic organisms.
<references/>
 
__TOC__
==About this Structure==
</StructureSection>
1WU9 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=1WU9 OCA].
 
==Reference==
Structural insights into the EB1-APC interaction., Honnappa S, John CM, Kostrewa D, Winkler FK, Steinmetz MO, EMBO J. 2005 Jan 26;24(2):261-9. Epub 2004 Dec 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15616574 15616574]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Honnappa, S.]]
[[Category: Honnappa S]]
[[Category: John, C M.]]
[[Category: John CM]]
[[Category: Kostrewa, D.]]
[[Category: Kostrewa D]]
[[Category: Steinmetz, M O.]]
[[Category: Steinmetz MO]]
[[Category: Winkler, F K.]]
[[Category: Winkler FK]]
[[Category: apc/dynactin binding domain]]
[[Category: coiled coil]]
[[Category: eb1-like structural motif]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:41:03 2008''

Latest revision as of 16:34, 13 March 2024

Crystal structure of the C-terminal domain of the end-binding protein 1 (EB1)Crystal structure of the C-terminal domain of the end-binding protein 1 (EB1)

Structural highlights

1wu9 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.54Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MARE1_HUMAN Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes cytoplasmic microtubule nucleation and elongation. May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes. May play a role in cell migration.[1] [2] [3] [4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Askham JM, Vaughan KT, Goodson HV, Morrison EE. Evidence that an interaction between EB1 and p150(Glued) is required for the formation and maintenance of a radial microtubule array anchored at the centrosome. Mol Biol Cell. 2002 Oct;13(10):3627-45. PMID:12388762 doi:10.1091/mbc.E02-01-0061
  2. ↑ van der Vaart B, Manatschal C, Grigoriev I, Olieric V, Gouveia SM, Bjelic S, Demmers J, Vorobjev I, Hoogenraad CC, Steinmetz MO, Akhmanova A. SLAIN2 links microtubule plus end-tracking proteins and controls microtubule growth in interphase. J Cell Biol. 2011 Jun 13;193(6):1083-99. Epub 2011 Jun 6. PMID:21646404 doi:10.1083/jcb.201012179
  3. ↑ Hayashi I, Wilde A, Mal TK, Ikura M. Structural basis for the activation of microtubule assembly by the EB1 and p150Glued complex. Mol Cell. 2005 Aug 19;19(4):449-60. PMID:16109370 doi:10.1016/j.molcel.2005.06.034
  4. ↑ Honnappa S, Gouveia SM, Weisbrich A, Damberger FF, Bhavesh NS, Jawhari H, Grigoriev I, van Rijssel FJ, Buey RM, Lawera A, Jelesarov I, Winkler FK, Wuthrich K, Akhmanova A, Steinmetz MO. An EB1-binding motif acts as a microtubule tip localization signal. Cell. 2009 Jul 23;138(2):366-76. PMID:19632184 doi:S0092-8674(09)00638-2

1wu9, resolution 1.54Å

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