View source for 4ytd


==Crystal structure of the C-terminal Coiled Coil of mouse Bicaudal D1==
<StructureSection load='4ytd' size='340' side='right'caption='[[4ytd]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ytd]] is a 2 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=4YTD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YTD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#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>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=4ytd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ytd OCA], [https://pdbe.org/4ytd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ytd RCSB], [https://www.ebi.ac.uk/pdbsum/4ytd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ytd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BICD1_MOUSE BICD1_MOUSE] Regulates coat complex coatomer protein I (COPI)-independent Golgi-endoplasmic reticulum transport by recruiting the dynein-dynactin motor complex.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bicaudal-D1 (BICD1) is an alpha-helical coiled-coil protein mediating the attachment of specific cargo to cytoplasmic dynein. It plays an essential role in minus end-directed intracellular transport along microtubules. The third C-terminal coiled-coil region of BICD1 (BICD1 CC3) has an important role in cargo sorting, including intracellular vesicles associating with the small GTPase Rab6 and the nuclear pore complex Ran binding protein 2 (RanBP2), and inhibiting the association with cytoplasmic dynein by binding to the first N-terminal coiled-coil region (CC1). The crystal structure of BICD1 CC3 revealed a parallel homodimeric coiled-coil with asymmetry and complementary knobs-into-holes interactions, differing from Drosophila BicD CC3. Furthermore, our binding study indicated that BICD1 CC3 possesses a binding surface for two distinct cargos, Rab6 and RanBP2, and that the CC1-binding site overlaps with the Rab6-binding site. These findings suggest a molecular basis for cargo recognition and autoinhibition of BICD proteins during dynein-dependent intracellular retrograde transport.

Structural basis for cargo binding and autoinhibition of Bicaudal-D1 by a parallel coiled-coil with homotypic registry.,Terawaki SI, Yoshikane A, Higuchi Y, Wakamatsu K Biochem Biophys Res Commun. 2015 Mar 18. pii: S0006-291X(15)00489-1. doi:, 10.1016/j.bbrc.2015.03.054. PMID:25796327<ref>PMID:25796327</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ytd" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Higuchi Y]]
[[Category: Terawaki S]]
[[Category: Wakamatsu K]]
[[Category: Yoshikane A]]