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| | <StructureSection load='4ytd' size='340' side='right'caption='[[4ytd]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='4ytd' size='340' side='right'caption='[[4ytd]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ytd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </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='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'>[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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Bicd1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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://pdbe.org/4ytd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ytd RCSB], [http://www.ebi.ac.uk/pdbsum/4ytd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ytd ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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. | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Higuchi, Y]] | + | [[Category: Higuchi Y]] |
| - | [[Category: Terawaki, S]] | + | [[Category: Terawaki S]] |
| - | [[Category: Wakamatsu, K]] | + | [[Category: Wakamatsu K]] |
| - | [[Category: Yoshikane, A]] | + | [[Category: Yoshikane A]] |
| - | [[Category: Bicaudal d1]]
| + | |
| - | [[Category: Cargo binding]]
| + | |
| - | [[Category: Coiled coil]]
| + | |
| - | [[Category: Cytoplasmic dynein]]
| + | |
| - | [[Category: Retrograde transport]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
BICD1_MOUSE Regulates coat complex coatomer protein I (COPI)-independent Golgi-endoplasmic reticulum transport by recruiting the dynein-dynactin motor complex.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Terawaki SI, Yoshikane A, Higuchi Y, Wakamatsu K. Structural basis for cargo binding and autoinhibition of Bicaudal-D1 by a parallel coiled-coil with homotypic registry. Biochem Biophys Res Commun. 2015 Mar 18. pii: S0006-291X(15)00489-1. doi:, 10.1016/j.bbrc.2015.03.054. PMID:25796327 doi:http://dx.doi.org/10.1016/j.bbrc.2015.03.054
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