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| | <StructureSection load='4rqm' size='340' side='right'caption='[[4rqm]], [[Resolution|resolution]] 1.75Å' scene=''> | | <StructureSection load='4rqm' size='340' side='right'caption='[[4rqm]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4rqm]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RQM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RQM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4rqm]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RQM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RQM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4rqn|4rqn]]</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=4rqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rqm OCA], [https://pdbe.org/4rqm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rqm RCSB], [https://www.ebi.ac.uk/pdbsum/4rqm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rqm ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BICC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4rqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rqm OCA], [http://pdbe.org/4rqm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rqm RCSB], [http://www.ebi.ac.uk/pdbsum/4rqm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rqm ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/BICC1_HUMAN BICC1_HUMAN]] Autosomal dominant polycystic kidney disease. Disease susceptibility is associated with variations affecting the gene represented in this entry. | + | [https://www.uniprot.org/uniprot/BICC1_HUMAN BICC1_HUMAN] Autosomal dominant polycystic kidney disease. Disease susceptibility is associated with variations affecting the gene represented in this entry. |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BICC1_HUMAN BICC1_HUMAN]] Putative RNA-binding protein. Acts as a negative regulator of Wnt signaling. May be involved in regulating gene expression during embryonic development.<ref>PMID:21922595</ref> | + | [https://www.uniprot.org/uniprot/BICC1_HUMAN BICC1_HUMAN] Putative RNA-binding protein. Acts as a negative regulator of Wnt signaling. May be involved in regulating gene expression during embryonic development.<ref>PMID:21922595</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bowie, J U]] | + | [[Category: Bowie JU]] |
| - | [[Category: Cascio, D]] | + | [[Category: Cascio D]] |
| - | [[Category: Leettola, C N]] | + | [[Category: Leettola CN]] |
| - | [[Category: P-body]]
| + | |
| - | [[Category: Polymerization]]
| + | |
| - | [[Category: Polymerization domain]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Protein-protein interaction domain]]
| + | |
| - | [[Category: Sam domain]]
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| Structural highlights
Disease
BICC1_HUMAN Autosomal dominant polycystic kidney disease. Disease susceptibility is associated with variations affecting the gene represented in this entry.
Function
BICC1_HUMAN Putative RNA-binding protein. Acts as a negative regulator of Wnt signaling. May be involved in regulating gene expression during embryonic development.[1]
Publication Abstract from PubMed
Head-to-tail polymers of sterile alpha motifs (SAM) can scaffold large macromolecular complexes. Several SAM-domain proteins that bind each other are mutated in patients with cystic kidneys or laterality defects, including the Ankyrin (ANK) and SAM domain-containing proteins ANKS6 and ANKS3, and the RNA-binding protein Bicc1. To address how their interactions are regulated, we first determined a high-resolution crystal structure of a Bicc1-SAM polymer, revealing a canonical SAM polymer with a high degree of flexibility in the subunit interface orientations. We further mapped interactions between full-length and distinct domains of Bicc1, ANKS3, and ANKS6. Neither ANKS3 nor ANKS6 alone formed macroscopic homopolymers in vivo. However, ANKS3 recruited ANKS6 to Bicc1, and the three proteins together cooperatively generated giant macromolecular complexes. Thus, the giant assemblies are shaped by SAM domains, their flanking sequences, and SAM-independent protein-protein and protein-mRNA interactions.
Crystal Structure of Bicc1 SAM Polymer and Mapping of Interactions between the Ciliopathy-Associated Proteins Bicc1, ANKS3, and ANKS6.,Rothe B, Leettola CN, Leal-Esteban L, Cascio D, Fortier S, Isenschmid M, Bowie JU, Constam DB Structure. 2018 Feb 6;26(2):209-224.e6. doi: 10.1016/j.str.2017.12.002. Epub 2017, Dec 28. PMID:29290488[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kraus MR, Clauin S, Pfister Y, Di Maio M, Ulinski T, Constam D, Bellanne-Chantelot C, Grapin-Botton A. Two mutations in human BICC1 resulting in Wnt pathway hyperactivity associated with cystic renal dysplasia. Hum Mutat. 2012 Jan;33(1):86-90. doi: 10.1002/humu.21610. Epub 2011 Oct 31. PMID:21922595 doi:http://dx.doi.org/10.1002/humu.21610
- ↑ Rothe B, Leettola CN, Leal-Esteban L, Cascio D, Fortier S, Isenschmid M, Bowie JU, Constam DB. Crystal Structure of Bicc1 SAM Polymer and Mapping of Interactions between the Ciliopathy-Associated Proteins Bicc1, ANKS3, and ANKS6. Structure. 2018 Feb 6;26(2):209-224.e6. doi: 10.1016/j.str.2017.12.002. Epub 2017, Dec 28. PMID:29290488 doi:http://dx.doi.org/10.1016/j.str.2017.12.002
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