5lzn
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==-TIP microtubule-binding domain== | |
| + | <StructureSection load='5lzn' size='340' side='right' caption='[[5lzn]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5lzn]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LZN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LZN FirstGlance]. <br> | ||
| + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5lzn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lzn OCA], [http://pdbe.org/5lzn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lzn RCSB], [http://www.ebi.ac.uk/pdbsum/5lzn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lzn ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/CAMP3_MOUSE CAMP3_MOUSE]] Microtubule minus-end binding protein that acts as a regulator of microtubule dynamics. Specifically required for zonula adherens biogenesis and maintenance by anchoring microtubules at their minus-ends to zonula adherens, leading to recruit KIFC3 kinesin to junctional site (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | CAMSAP and Patronin family members regulate microtubule minus-end stability and localization and thus organize noncentrosomal microtubule networks, which are essential for cell division, polarization and differentiation. Here, we found that the CAMSAP C-terminal CKK domain is widely present among eukaryotes and autonomously recognizes microtubule minus ends. Through a combination of structural approaches, we uncovered how mammalian CKK binds between two tubulin dimers at the interprotofilament interface on the outer microtubule surface. In vitro reconstitution assays combined with high-resolution fluorescence microscopy and cryo-electron tomography suggested that CKK preferentially associates with the transition zone between curved protofilaments and the regular microtubule lattice. We propose that minus-end-specific features of the interprotofilament interface at this site serve as the basis for CKK's minus-end preference. The steric clash between microtubule-bound CKK and kinesin motors explains how CKK protects microtubule minus ends against kinesin-13-induced depolymerization and thus controls the stability of free microtubule minus ends. | ||
| - | + | A structural model for microtubule minus-end recognition and protection by CAMSAP proteins.,Atherton J, Jiang K, Stangier MM, Luo Y, Hua S, Houben K, van Hooff JJE, Joseph AP, Scarabelli G, Grant BJ, Roberts AJ, Topf M, Steinmetz MO, Baldus M, Moores CA, Akhmanova A Nat Struct Mol Biol. 2017 Oct 9. doi: 10.1038/nsmb.3483. PMID:28991265<ref>PMID:28991265</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5lzn" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Stangier, M M]] | ||
| + | [[Category: Steinmetz, M O]] | ||
| + | [[Category: Tip]] | ||
| + | [[Category: Microtubule]] | ||
| + | [[Category: Structural protein]] | ||
Revision as of 07:01, 18 October 2017
-TIP microtubule-binding domain
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