4ytd: Difference between revisions
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''' | ==Crystal structure of the C-terminal Coiled Coil of mouse Bicaudal D1== | ||
<StructureSection load='4ytd' size='340' side='right' caption='[[4ytd]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ytd]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YTD FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4ytd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ytd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ytd RCSB], [http://www.ebi.ac.uk/pdbsum/4ytd PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Higuchi, Y]] | [[Category: Higuchi, Y]] | ||
[[Category: Terawaki, S]] | |||
[[Category: Wakamatsu, K]] | |||
[[Category: Yoshikane, A]] | [[Category: Yoshikane, A]] | ||
[[Category: | [[Category: Bicaudal d1]] | ||
[[Category: | [[Category: Cargo binding]] | ||
[[Category: Coiled coil]] | |||
[[Category: Cytoplasmic dynein]] | |||
[[Category: Retrograde transport]] | |||
Revision as of 11:02, 8 April 2015
Crystal structure of the C-terminal Coiled Coil of mouse Bicaudal D1
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