5b22: Difference between revisions

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<StructureSection load='5b22' size='340' side='right'caption='[[5b22]], [[Resolution|resolution]] 2.58&Aring;' scene=''>
<StructureSection load='5b22' size='340' side='right'caption='[[5b22]], [[Resolution|resolution]] 2.58&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5b22]] 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=5B22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B22 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5b22]] 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=5B22 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B22 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5b21|5b21]]</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=5b22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b22 OCA], [https://pdbe.org/5b22 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b22 RCSB], [https://www.ebi.ac.uk/pdbsum/5b22 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b22 ProSAT]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Nectin3, Pvrl3 ([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=5b22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b22 OCA], [http://pdbe.org/5b22 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b22 RCSB], [http://www.ebi.ac.uk/pdbsum/5b22 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b22 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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>
[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>  


==See Also==
==See Also==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lk3 transgenic mice]]
[[Category: Mus musculus]]
[[Category: Katsutani, T]]
[[Category: Katsutani T]]
[[Category: Narita, H]]
[[Category: Narita H]]
[[Category: Sangawa, T]]
[[Category: Sangawa T]]
[[Category: Suzuki, M]]
[[Category: Suzuki M]]
[[Category: Takebe, K]]
[[Category: Takebe K]]
[[Category: Adherens janction]]
[[Category: Cell adhesion]]
[[Category: Cell-adhesion]]
[[Category: Immuboglobulin-like domain]]

Revision as of 09:36, 31 May 2023

Dimer structure of murine Nectin-3 D1D2Dimer structure of murine Nectin-3 D1D2

Structural highlights

5b22 is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2] [3] [4] [5]

See Also

References

  1. ↑ Satoh-Horikawa K, Nakanishi H, Takahashi K, Miyahara M, Nishimura M, Tachibana K, Mizoguchi A, Takai Y. Nectin-3, a new member of immunoglobulin-like cell adhesion molecules that shows homophilic and heterophilic cell-cell adhesion activities. J Biol Chem. 2000 Apr 7;275(14):10291-9. PMID:10744716
  2. ↑ Mizoguchi A, Nakanishi H, Kimura K, Matsubara K, Ozaki-Kuroda K, Katata T, Honda T, Kiyohara Y, Heo K, Higashi M, Tsutsumi T, Sonoda S, Ide C, Takai Y. Nectin: an adhesion molecule involved in formation of synapses. J Cell Biol. 2002 Feb 4;156(3):555-65. Epub 2002 Feb 4. PMID:11827984 doi:http://dx.doi.org/10.1083/jcb.200103113
  3. ↑ Ozaki-Kuroda K, Nakanishi H, Ohta H, Tanaka H, Kurihara H, Mueller S, Irie K, Ikeda W, Sakai T, Wimmer E, Nishimune Y, Takai Y. Nectin couples cell-cell adhesion and the actin scaffold at heterotypic testicular junctions. Curr Biol. 2002 Jul 9;12(13):1145-50. PMID:12121624
  4. ↑ Honda T, Shimizu K, Kawakatsu T, Yasumi M, Shingai T, Fukuhara A, Ozaki-Kuroda K, Irie K, Nakanishi H, Takai Y. Antagonistic and agonistic effects of an extracellular fragment of nectin on formation of E-cadherin-based cell-cell adhesion. Genes Cells. 2003 Jan;8(1):51-63. PMID:12558799
  5. ↑ Sato T, Irie K, Okamoto R, Ooshio T, Fujita N, Takai Y. Common signaling pathway is used by the trans-interaction of Necl-5/Tage4/PVR/CD155 and nectin, and of nectin and nectin during the formation of cell-cell adhesion. Cancer Sci. 2005 Sep;96(9):578-89. PMID:16128743 doi:http://dx.doi.org/CAS087

5b22, resolution 2.58Å

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