7wek: Difference between revisions

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'''Unreleased structure'''


The entry 7wek is ON HOLD  until Paper Publication
==Crystal structure of the mouse Wdr47 NTD in complex with the WBR motif form Camsap3.==
<StructureSection load='7wek' size='340' side='right'caption='[[7wek]], [[Resolution|resolution]] 3.21&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7wek]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WEK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WEK FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7wek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wek OCA], [https://pdbe.org/7wek PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wek RCSB], [https://www.ebi.ac.uk/pdbsum/7wek PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wek ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/WDR47_MOUSE WDR47_MOUSE]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Calmodulin-regulated spectrin-associated proteins (Camsaps) bind to the N-terminal domain of WD40-repeat 47 (Wdr47-NTD; featured with a LisH-CTLH motif) to properly generate axonemal central-pair microtubules (CP-MTs) for the planar beat pattern of mammalian motile multicilia. The underlying molecular mechanism, however, remains unclear. Here, we determine the structures of apo-Wdr47-NTD and Wdr47-NTD in complex with a characteristic Wdr47-binding region (WBR) from Camsap3. Wdr47-NTD forms an intertwined dimer with a special cross-over region (COR) in addition to the canonical LisH and globular alpha-helical core (GAC). The basic WBR peptide adopts an alpha-helical conformation and anchors to a tailored acidic pocket embedded in the COR. Mutations in this target-binding pocket disrupt the interaction between Wdr47-NTD and Camsap3. Impairing Wdr47-Camsap interactions markedly reduces rescue effects of Wdr47 on CP-MTs and ciliary beat of Wdr47-deficient ependymal cells. Thus, Wdr47-NTD functions by recognizing a specific basic helical motif in Camsap proteins via its non-canonical COR, a target-binding site in LisH-CTLH-containing domains.


Authors: Ren, J.Q., Li, D., Feng, W.
Intertwined Wdr47-NTD dimer recognizes a basic-helical motif in Camsap proteins for proper central-pair microtubule formation.,Ren J, Li D, Liu J, Liu H, Yan X, Zhu X, Feng W Cell Rep. 2022 Nov 8;41(6):111589. doi: 10.1016/j.celrep.2022.111589. PMID:36351391<ref>PMID:36351391</ref>


Description: Crystal structure of the mouse Wdr47 NTD in complex with the WBR motif form Camsap3.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Li, D]]
<div class="pdbe-citations 7wek" style="background-color:#fffaf0;"></div>
[[Category: Ren, J.Q]]
== References ==
[[Category: Feng, W]]
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Feng W]]
[[Category: Li D]]
[[Category: Ren JQ]]
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