6cmx: Difference between revisions

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~~'''Unreleased structure'''~~

The ~~entry 6cmx~~ is ~~ON HOLD~~

==Human Teneurin 2 extra-cellular region==

== Structural highlights ==

<table><tr><td colspan='2'>[[6cmx]] is a 1 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=6CMX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CMX FirstGlance]. <br>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.1Å</td></tr>

<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900118:6alpha-alpha-mannobiose'>PRD_900118</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=6cmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cmx OCA], [https://pdbe.org/6cmx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cmx RCSB], [https://www.ebi.ac.uk/pdbsum/6cmx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cmx ProSAT]</span></td></tr>

</table>

== Function ==

[https://www.uniprot.org/uniprot/TEN2_HUMAN TEN2_HUMAN] Involved in neural development, regulating the establishment of proper connectivity within the nervous system. Promotes the formation of filopodia and enlarged growth cone in neuronal cells. Induces homophilic cell-cell adhesion (By similarity). May function as a cellular signal transducer.<ref>PMID:21724987</ref> Acts as a ligand of the ADGRL1 receptor. Mediates axon guidance and heterophilic cell-cell adhesion.<ref>PMID:21724987</ref> Induces gene transcription inhibition.

== Publication Abstract from PubMed ==

Teneurins (TENs) are cell-surface adhesion proteins with critical roles in tissue development and axon guidance. Here, we report the 3.1-A cryoelectron microscopy structure of the human TEN2 extracellular region (ECR), revealing a striking similarity to bacterial Tc-toxins. The ECR includes a large beta barrel that partially encapsulates a C-terminal domain, which emerges to the solvent through an opening in the mid-barrel region. An immunoglobulin (Ig)-like domain seals the bottom of the barrel while a beta propeller is attached in a perpendicular orientation. We further show that an alternatively spliced region within the beta propeller acts as a switch to regulate trans-cellular adhesion of TEN2 to latrophilin (LPHN), a transmembrane receptor known to mediate critical functions in the central nervous system. One splice variant activates trans-cellular signaling in a LPHN-dependent manner, whereas the other induces inhibitory postsynaptic differentiation. These results highlight the unusual structural organization of TENs giving rise to their multifarious functions.

~~Authors~~:

, PMID:29677516<ref>PMID:29677516</ref>

~~Description~~:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased~~ Structures]]

</div>

== References ==

__TOC__

</SX>

[[Category: Homo sapiens]]

[[Category: Large Structures]]

[[Category: Arac D]]

[[Category: Li J]]

[[Category: Shalev-Benami M]]

[[Category: Skiniotis G]]

[[Category: Sudhof T]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6cmx is ON HOLD
+==Human Teneurin 2 extra-cellular region==
+<SX load='6cmx' size='340' side='right' viewer='molstar' caption='[[6cmx]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6cmx]] is a 1 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=6CMX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CMX FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900118:6alpha-alpha-mannobiose'>PRD_900118</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=6cmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cmx OCA], [https://pdbe.org/6cmx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cmx RCSB], [https://www.ebi.ac.uk/pdbsum/6cmx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cmx ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TEN2_HUMAN TEN2_HUMAN] Involved in neural development, regulating the establishment of proper connectivity within the nervous system. Promotes the formation of filopodia and enlarged growth cone in neuronal cells. Induces homophilic cell-cell adhesion (By similarity). May function as a cellular signal transducer.<ref>PMID:21724987</ref>   Acts as a ligand of the ADGRL1 receptor. Mediates axon guidance and heterophilic cell-cell adhesion.<ref>PMID:21724987</ref>   Induces gene transcription inhibition.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Teneurins (TENs) are cell-surface adhesion proteins with critical roles in tissue development and axon guidance. Here, we report the 3.1-A cryoelectron microscopy structure of the human TEN2 extracellular region (ECR), revealing a striking similarity to bacterial Tc-toxins. The ECR includes a large beta barrel that partially encapsulates a C-terminal domain, which emerges to the solvent through an opening in the mid-barrel region. An immunoglobulin (Ig)-like domain seals the bottom of the barrel while a beta propeller is attached in a perpendicular orientation. We further show that an alternatively spliced region within the beta propeller acts as a switch to regulate trans-cellular adhesion of TEN2 to latrophilin (LPHN), a transmembrane receptor known to mediate critical functions in the central nervous system. One splice variant activates trans-cellular signaling in a LPHN-dependent manner, whereas the other induces inhibitory postsynaptic differentiation. These results highlight the unusual structural organization of TENs giving rise to their multifarious functions.
-Authors:
+,  PMID:29677516<ref>PMID:29677516</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6cmx" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</SX>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Arac D]]
+[[Category: Li J]]
+[[Category: Shalev-Benami M]]
+[[Category: Skiniotis G]]
+[[Category: Sudhof T]]