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6fc5

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'''Unreleased structure'''
 
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The entry 6fc5 is ON HOLD
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==Bik1 CAP-Gly domain==
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<StructureSection load='6fc5' size='340' side='right' caption='[[6fc5]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Kumar, A., Stangier, M.M., Steinmetz, M.O.
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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>
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Description: Bik1 CAP-Gly domain
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6fc5" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Kumar, A]]
[[Category: Kumar, A]]
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[[Category: Steinmetz, M.O]]
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[[Category: Stangier, M M]]
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[[Category: Stangier, M.M]]
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[[Category: Steinmetz, M O]]
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[[Category: Tip]]
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[[Category: Cap-gly]]
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[[Category: Cell cycle]]
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[[Category: Microtubule]]
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[[Category: Yeast]]

Revision as of 13:57, 11 April 2018

Bik1 CAP-Gly domain

6fc5, resolution 1.88Å

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