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| <StructureSection load='4r11' size='340' side='right'caption='[[4r11]], [[Resolution|resolution]] 2.79Å' scene=''> | | <StructureSection load='4r11' size='340' side='right'caption='[[4r11]], [[Resolution|resolution]] 2.79Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[4r11]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R11 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R11 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4r11]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R11 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R11 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr> |
- | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</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=4r11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r11 OCA], [https://pdbe.org/4r11 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r11 RCSB], [https://www.ebi.ac.uk/pdbsum/4r11 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r11 ProSAT]</span></td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4r0z|4r0z]], [[4r10|4r10]]</td></tr>
| + | |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hmp-2, K05C4.6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL]), hmr-1, W02B9.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</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=4r11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r11 OCA], [http://pdbe.org/4r11 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r11 RCSB], [http://www.ebi.ac.uk/pdbsum/4r11 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r11 ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/HMP2_CAEEL HMP2_CAEEL]] Required for cell migration during body enclosure and cell shape changes during body elongation.<ref>PMID:9531567</ref> [[http://www.uniprot.org/uniprot/HMR1_CAEEL HMR1_CAEEL]] Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. Isoform A is required for cell migration during body enclosure and cell shape changes during body elongation. Required for proper localization of other junctional components, such as hmp-1, hmp-2 and jac-1. Isoform b is involved in axonal guidance in a subset of motor neurons.<ref>PMID:11790304</ref> <ref>PMID:12847081</ref> <ref>PMID:9531567</ref> | + | [https://www.uniprot.org/uniprot/HMP2_CAEEL HMP2_CAEEL] Required for cell migration during body enclosure and cell shape changes during body elongation.<ref>PMID:9531567</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: Caeel]] | + | [[Category: Caenorhabditis elegans]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Bang, I]] | + | [[Category: Bang I]] |
- | [[Category: Choi, H J]] | + | [[Category: Choi H-J]] |
- | [[Category: Hardin, J]] | + | [[Category: Hardin J]] |
- | [[Category: Loveless, T]] | + | [[Category: Loveless T]] |
- | [[Category: Lynch, A]] | + | [[Category: Lynch A]] |
- | [[Category: Weis, W I]] | + | [[Category: Weis WI]] |
- | [[Category: Armadillo repeat]]
| + | |
- | [[Category: Cell adhesion]]
| + | |
- | [[Category: Cell adhesion-protein binding complex]]
| + | |
- | [[Category: Phosphorylation]]
| + | |
| Structural highlights
Function
HMP2_CAEEL Required for cell migration during body enclosure and cell shape changes during body elongation.[1]
Publication Abstract from PubMed
In metazoan adherens junctions, beta-catenin links the cytoplasmic tail of classical cadherins to the F-actin-binding protein alpha-catenin. Phosphorylation of a Ser/Thr-rich region in the cadherin tail dramatically enhances affinity for beta-catenin and promotes cell-cell adhesion in cell culture systems, but its importance has not been demonstrated in vivo. Here, we identify a critical phosphorylated serine in the C. elegans cadherin HMR-1 required for strong binding to the beta-catenin homolog HMP-2. Ablation of this phosphoserine interaction produces developmental defects that resemble full loss-of-function (Hammerhead and Humpback) phenotypes. Most metazoans possess a single gene for beta-catenin, which is also a transcriptional coactivator in Wnt signaling. Nematodes and planaria, however, have a set of paralogous beta-catenins; for example, C. elegans HMP-2 functions only in cell-cell adhesion, whereas SYS-1 mediates transcriptional activation through interactions with POP-1/Tcf. Our structural data define critical sequence differences responsible for the unique ligand specificities of these two proteins.
A Conserved Phosphorylation Switch Controls the Interaction between Cadherin and beta-Catenin In Vitro and In Vivo.,Choi HJ, Loveless T, Lynch AM, Bang I, Hardin J, Weis WI Dev Cell. 2015 Apr 6;33(1):82-93. doi: 10.1016/j.devcel.2015.02.005. PMID:25850673[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Costa M, Raich W, Agbunag C, Leung B, Hardin J, Priess JR. A putative catenin-cadherin system mediates morphogenesis of the Caenorhabditis elegans embryo. J Cell Biol. 1998 Apr 6;141(1):297-308. PMID:9531567
- ↑ Choi HJ, Loveless T, Lynch AM, Bang I, Hardin J, Weis WI. A Conserved Phosphorylation Switch Controls the Interaction between Cadherin and beta-Catenin In Vitro and In Vivo. Dev Cell. 2015 Apr 6;33(1):82-93. doi: 10.1016/j.devcel.2015.02.005. PMID:25850673 doi:http://dx.doi.org/10.1016/j.devcel.2015.02.005
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