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3axa

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==Crystal structure of afadin PDZ domain in complex with the C-terminal peptide from nectin-3==
==Crystal structure of afadin PDZ domain in complex with the C-terminal peptide from nectin-3==
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<StructureSection load='3axa' size='340' side='right' caption='[[3axa]], [[Resolution|resolution]] 2.78&Aring;' scene=''>
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<StructureSection load='3axa' size='340' side='right'caption='[[3axa]], [[Resolution|resolution]] 2.78&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3axa]] 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=3AXA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AXA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3axa]] 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=3AXA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AXA FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Mllt4, Af6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.78&#8491;</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=3axa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3axa OCA], [http://pdbe.org/3axa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3axa RCSB], [http://www.ebi.ac.uk/pdbsum/3axa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3axa ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3axa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3axa OCA], [https://pdbe.org/3axa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3axa RCSB], [https://www.ebi.ac.uk/pdbsum/3axa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3axa ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/AFAD_MOUSE AFAD_MOUSE]] Belongs to an adhesion system, probably together with the E-cadherin-catenin system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs). Nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton. May play a key role in the organization of epithelial structures of the embryonic ectoderm.<ref>PMID:10477764</ref>
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[https://www.uniprot.org/uniprot/AFAD_MOUSE AFAD_MOUSE] Belongs to an adhesion system, probably together with the E-cadherin-catenin system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs). Nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton. May play a key role in the organization of epithelial structures of the embryonic ectoderm.<ref>PMID:10477764</ref> [https://www.uniprot.org/uniprot/NECT3_MOUSE NECT3_MOUSE] Plays a role in cell-cell adhesion through heterophilic trans-interactions with nectins-like or other nectins, such as trans-interaction with NECTIN2 at Sertoli-spermatid junctions. Trans-interaction with PVR induces activation of CDC42 and RAC small G proteins through common signaling molecules such as SRC and RAP1. Also involved in the formation of cell-cell junctions, including adherens junctions and synapses. Induces endocytosis-mediated down-regulation of PVR from the cell surface, resulting in reduction of cell movement and proliferation. Plays a role in the morphology of the ciliary body.<ref>PMID:10744716</ref> <ref>PMID:11827984</ref> <ref>PMID:12121624</ref> <ref>PMID:12558799</ref> <ref>PMID:16128743</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>
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[[Category: Lk3 transgenic mice]]
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[[Category: Large Structures]]
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[[Category: Fujiwara, Y]]
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[[Category: Mus musculus]]
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[[Category: Goda, N]]
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[[Category: Fujiwara Y]]
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[[Category: Hiroaki, H]]
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[[Category: Goda N]]
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[[Category: Nakagawa, A]]
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[[Category: Hiroaki H]]
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[[Category: Narita, H]]
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[[Category: Nakagawa A]]
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[[Category: Sakisaka, T]]
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[[Category: Narita H]]
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[[Category: Satomura, K]]
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[[Category: Sakisaka T]]
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[[Category: Suzuki, M]]
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[[Category: Satomura K]]
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[[Category: Af-6]]
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[[Category: Suzuki M]]
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[[Category: Cell adhesion]]
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[[Category: Fusion protein]]
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[[Category: Pdz domain]]
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Current revision

Crystal structure of afadin PDZ domain in complex with the C-terminal peptide from nectin-3

PDB ID 3axa

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