5xa5

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==Crystal structure of HMP-1-HMP-2 complex==
==Crystal structure of HMP-1-HMP-2 complex==
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<StructureSection load='5xa5' size='340' side='right' caption='[[5xa5]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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<StructureSection load='5xa5' size='340' side='right'caption='[[5xa5]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5xa5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XA5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XA5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5xa5]] is a 2 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=5XA5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XA5 FirstGlance]. <br>
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</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=5xa5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xa5 OCA], [http://pdbe.org/5xa5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xa5 RCSB], [http://www.ebi.ac.uk/pdbsum/5xa5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xa5 ProSAT]</span></td></tr>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hmp-1, R13H4.4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL]), hmp-2, K05C4.6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</td></tr>
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<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=5xa5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xa5 OCA], [http://pdbe.org/5xa5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xa5 RCSB], [http://www.ebi.ac.uk/pdbsum/5xa5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xa5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/HMP1_CAEEL HMP1_CAEEL]] Required for cell migration during body enclosure and cell shape changes during body elongation (PubMed:9531567). Required for proper localization of other junctional components, such as pac-1 (PubMed:25938815).<ref>PMID:25938815</ref> <ref>PMID:9531567</ref> [[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/HMP1_CAEEL HMP1_CAEEL]] Required for cell migration during body enclosure and cell shape changes during body elongation (PubMed:9531567). Required for proper localization of other junctional components, such as pac-1 (PubMed:25938815).<ref>PMID:25938815</ref> <ref>PMID:9531567</ref> [[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Stable tissue integrity during embryonic development relies on the function of the cadherin.catenin complex (CCC). The Caenorhabditis elegans CCC is a useful paradigm for analyzing in vivo requirements for specific interactions among the core components of the CCC, and it provides a unique opportunity to examine evolutionarily conserved mechanisms that govern the interaction between alpha- and beta-catenin. HMP-1, unlike its mammalian homolog alpha-catenin, is constitutively monomeric, and its binding affinity for HMP-2/beta-catenin is higher than that of alpha-catenin for beta-catenin. A crystal structure shows that the HMP-1.HMP-2 complex forms a five-helical bundle structure distinct from the structure of the mammalian alpha-catenin.beta-catenin complex. Deletion analysis based on the crystal structure shows that the first helix of HMP-1 is necessary for binding HMP-2 avidly in vitro and for efficient recruitment of HMP-1 to adherens junctions in embryos. HMP-2 Ser-47 and Tyr-69 flank its binding interface with HMP-1, and we show that phosphomimetic mutations at these two sites decrease binding affinity of HMP-1 to HMP-2 by 40-100-fold in vitro. In vivo experiments using HMP-2 S47E and Y69E mutants showed that they are unable to rescue hmp-2(zu364) mutants, suggesting that phosphorylation of HMP-2 on Ser-47 and Tyr-69 could be important for regulating CCC formation in C. elegans Our data provide novel insights into how cadherin-dependent cell-cell adhesion is modulated in metazoans by conserved elements as well as features unique to specific organisms.
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Cell-cell adhesion in metazoans relies on evolutionarily conserved features of the alpha-catenin.beta-catenin-binding interface.,Shao X, Kang H, Loveless T, Lee GR, Seok C, Weis WI, Choi HJ, Hardin J J Biol Chem. 2017 Oct 6;292(40):16477-16490. doi: 10.1074/jbc.M117.795567. Epub, 2017 Aug 25. PMID:28842483<ref>PMID:28842483</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5xa5" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Caeel]]
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[[Category: Large Structures]]
[[Category: Choi, H J]]
[[Category: Choi, H J]]
[[Category: Hardin, J]]
[[Category: Hardin, J]]

Revision as of 12:40, 25 December 2019

Crystal structure of HMP-1-HMP-2 complex

PDB ID 5xa5

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