2qk1
From Proteopedia
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| - | [[Image:2qk1.jpg|left|200px]] | + | [[Image:2qk1.jpg|left|200px]] |
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| - | '''Structural Basis of Microtubule Plus End Tracking by XMAP215, CLIP-170 and EB1''' | + | {{Structure |
| + | |PDB= 2qk1 |SIZE=350|CAPTION= <scene name='initialview01'>2qk1</scene>, resolution 1.700Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= STU2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | }} | ||
| + | |||
| + | '''Structural Basis of Microtubule Plus End Tracking by XMAP215, CLIP-170 and EB1''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2QK1 is a [ | + | 2QK1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QK1 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17889670 17889670] |
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: xmap215]] | [[Category: xmap215]] | ||
| - | ''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 18:26:41 2008'' |
Revision as of 16:26, 20 March 2008
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| , resolution 1.700Å | |||||||
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| Gene: | STU2 (Saccharomyces cerevisiae) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
2QK1 is a Single protein structure of sequence from Saccharomyces cerevisiae. 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 Thu Mar 20 18:26:41 2008
Categories: Saccharomyces cerevisiae | Single protein | Slep, K C. | Vale, R D. | +tip | Ch-tog | Dis1 | Heat repeat | Microtubule plus end | Protein binding | Stu2 | Stu2p | Tog | Xmap215
