6fc5: Difference between revisions
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The | ==Bik1 CAP-Gly domain== | ||
<StructureSection load='6fc5' size='340' side='right' caption='[[6fc5]], [[Resolution|resolution]] 1.88Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6fc5]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FC5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FC5 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=6fc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fc5 OCA], [http://pdbe.org/6fc5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fc5 RCSB], [http://www.ebi.ac.uk/pdbsum/6fc5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fc5 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In budding yeast, the microtubule plus-end tracking proteins Bik1 (CLIP-170) and Bim1 (EB1) form a complex that interacts with partners involved in spindle positioning, including Stu2 and Kar9. Here, we show that the CAP-Gly and coiled-coil domains of Bik1 interact with the C-terminal ETF peptide of Bim1 and the C-terminal tail region of Stu2, respectively. The crystal structures of the CAP-Gly domain of Bik1 (Bik1CG) alone and in complex with an ETF peptide revealed unique, functionally relevant CAP-Gly elements, establishing Bik1CG as a specific C-terminal phenylalanine recognition domain. Unlike the mammalian CLIP-170-EB1 complex, Bik1-Bim1 forms ternary complexes with the EB1-binding motifs SxIP and LxxPTPh, which are present in diverse proteins, including Kar9. Perturbation of the Bik1-Bim1 interaction in vivo affected Bik1 localization and astral microtubule length. Our results provide insight into the role of the Bik1-Bim1 interaction for cell division, and demonstrate that the CLIP-170-EB1 module is evolutionarily flexible. | |||
Structure-Function Relationship of the Bik1-Bim1 Complex.,Stangier MM, Kumar A, Chen X, Farcas AM, Barral Y, Steinmetz MO Structure. 2018 Apr 3;26(4):607-618.e4. doi: 10.1016/j.str.2018.03.003. Epub 2018, Mar 22. PMID:29576319<ref>PMID:29576319</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6fc5" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Kumar, A]] | [[Category: Kumar, A]] | ||
[[Category: Steinmetz, M | [[Category: Stangier, M M]] | ||
[[Category: | [[Category: Steinmetz, M O]] | ||
[[Category: Tip]] | |||
[[Category: Cap-gly]] | |||
[[Category: Cell cycle]] | |||
[[Category: Microtubule]] | |||
[[Category: Yeast]] | |||
