2qjz

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[[Image:2qjz.gif|left|200px]]
[[Image:2qjz.gif|left|200px]]
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{{Structure
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|PDB= 2qjz |SIZE=350|CAPTION= <scene name='initialview01'>2qjz</scene>, resolution 1.250&Aring;
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The line below this paragraph, containing "STRUCTURE_2qjz", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|GENE= MAPRE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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{{STRUCTURE_2qjz| PDB=2qjz | SCENE= }}
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|RELATEDENTRY=[[2qjx|2QJX]], [[2qk0|2QK0]], [[2qk1|2QK1]], [[2qk2|2QK2]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qjz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qjz OCA], [http://www.ebi.ac.uk/pdbsum/2qjz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qjz RCSB]</span>
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'''Structural Basis of Microtubule Plus End Tracking by XMAP215, CLIP-170 and EB1'''
'''Structural Basis of Microtubule Plus End Tracking by XMAP215, CLIP-170 and EB1'''
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[[Category: Vale, R D.]]
[[Category: Vale, R D.]]
[[Category: +tip]]
[[Category: +tip]]
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[[Category: calponin homology domain]]
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[[Category: Calponin homology domain]]
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[[Category: eb1]]
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[[Category: Eb1]]
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[[Category: microtubule plus end]]
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[[Category: Microtubule plus end]]
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[[Category: protein binding]]
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[[Category: Protein binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 15:05:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:50:07 2008''
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Revision as of 12:05, 4 May 2008

Template:STRUCTURE 2qjz

Structural Basis of Microtubule Plus End Tracking by XMAP215, CLIP-170 and EB1


Overview

Microtubule plus end binding proteins (+TIPs) localize to the dynamic plus ends of microtubules, where they stimulate microtubule growth and recruit signaling molecules. Three main +TIP classes have been identified (XMAP215, EB1, and CLIP-170), but whether they act upon microtubule plus ends through a similar mechanism has not been resolved. Here, we report crystal structures of the tubulin binding domains of XMAP215 (yeast Stu2p and Drosophila Msps), EB1 (yeast Bim1p and human EB1), and CLIP-170 (human), which reveal diverse tubulin binding interfaces. Functional studies, however, reveal a common property that native or artificial dimerization of tubulin binding domains (including chemically induced heterodimers of EB1 and CLIP-170) induces tubulin nucleation/assembly in vitro and, in most cases, plus end tracking in living cells. We propose that +TIPs, although diverse in structure, share a common property of multimerizing tubulin, thus acting as polymerization chaperones that aid in subunit addition to the microtubule plus end.

About this Structure

2QJZ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis of microtubule plus end tracking by XMAP215, CLIP-170, and EB1., Slep KC, Vale RD, Mol Cell. 2007 Sep 21;27(6):976-91. PMID:17889670 Page seeded by OCA on Sun May 4 15:05:26 2008

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