2qk1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (05:28, 17 October 2024) (edit) (undo)
 
(9 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:2qk1.png|left|200px]]
 
-
<!--
+
==Structural Basis of Microtubule Plus End Tracking by XMAP215, CLIP-170 and EB1==
-
The line below this paragraph, containing "STRUCTURE_2qk1", creates the "Structure Box" on the page.
+
<StructureSection load='2qk1' size='340' side='right'caption='[[2qk1]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[2qk1]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QK1 FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-
{{STRUCTURE_2qk1| PDB=2qk1 | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qk1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qk1 OCA], [https://pdbe.org/2qk1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qk1 RCSB], [https://www.ebi.ac.uk/pdbsum/2qk1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qk1 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/STU2_YEAST STU2_YEAST] May play a role in the attachment, organization, and/or dynamics of microtubule ends at the spindle pole body.
 +
== 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/qk/2qk1_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2qk1 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
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.
-
===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.,Slep KC, Vale RD Mol Cell. 2007 Sep 21;27(6):976-91. PMID:17889670<ref>PMID:17889670</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_17889670}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 2qk1" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 17889670 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_17889670}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Large Structures]]
-
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==
+
-
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: Slep KC]]
-
[[Category: Slep, K C.]]
+
[[Category: Vale RD]]
-
[[Category: Vale, R D.]]
+
-
[[Category: +tip]]
+
-
[[Category: Ch-tog]]
+
-
[[Category: Dis1]]
+
-
[[Category: Heat repeat]]
+
-
[[Category: Microtubule plus end]]
+
-
[[Category: Protein binding]]
+
-
[[Category: Stu2]]
+
-
[[Category: Stu2p]]
+
-
[[Category: Tog]]
+
-
[[Category: Xmap215]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:04:58 2008''
+

Current revision

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

PDB ID 2qk1

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools