6cmx: Difference between revisions

Revision as of 07:52, 17 October 2024

Human Teneurin 2 extra-cellular region

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Structural highlights

6cmx is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.1Å
Ligands:	MAN, NAG, PRD_900118
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] Acts as a ligand of the ADGRL1 receptor. Mediates axon guidance and heterophilic cell-cell adhesion.^[2] 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.

Structural Basis for Teneurin Function in Circuit-Wiring: A Toxin Motif at the Synapse.,Li J, Shalev-Benami M, Sando R, Jiang X, Kibrom A, Wang J, Leon K, Katanski C, Nazarko O, Lu YC, Sudhof TC, Skiniotis G, Arac D Cell. 2018 Apr 19;173(3):735-748.e15. doi: 10.1016/j.cell.2018.03.036. PMID:29677516^[3]

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

References

↑ Silva JP, Lelianova VG, Ermolyuk YS, Vysokov N, Hitchen PG, Berninghausen O, Rahman MA, Zangrandi A, Fidalgo S, Tonevitsky AG, Dell A, Volynski KE, Ushkaryov YA. Latrophilin 1 and its endogenous ligand Lasso/teneurin-2 form a high-affinity transsynaptic receptor pair with signaling capabilities. Proc Natl Acad Sci U S A. 2011 Jul 19;108(29):12113-8. doi:, 10.1073/pnas.1019434108. Epub 2011 Jul 1. PMID:21724987 doi:https://dx.doi.org/10.1073/pnas.1019434108
↑ Silva JP, Lelianova VG, Ermolyuk YS, Vysokov N, Hitchen PG, Berninghausen O, Rahman MA, Zangrandi A, Fidalgo S, Tonevitsky AG, Dell A, Volynski KE, Ushkaryov YA. Latrophilin 1 and its endogenous ligand Lasso/teneurin-2 form a high-affinity transsynaptic receptor pair with signaling capabilities. Proc Natl Acad Sci U S A. 2011 Jul 19;108(29):12113-8. doi:, 10.1073/pnas.1019434108. Epub 2011 Jul 1. PMID:21724987 doi:https://dx.doi.org/10.1073/pnas.1019434108
↑ Li J, Shalev-Benami M, Sando R, Jiang X, Kibrom A, Wang J, Leon K, Katanski C, Nazarko O, Lu YC, Sudhof TC, Skiniotis G, Arac D. Structural Basis for Teneurin Function in Circuit-Wiring: A Toxin Motif at the Synapse. Cell. 2018 Apr 19;173(3):735-748.e15. doi: 10.1016/j.cell.2018.03.036. PMID:29677516 doi:https://dx.doi.org/10.1016/j.cell.2018.03.036

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Silva JP, Lelianova VG, Ermolyuk YS, Vysokov N, Hitchen PG, Berninghausen O, Rahman MA, Zangrandi A, Fidalgo S, Tonevitsky AG, Dell A, Volynski KE, Ushkaryov YA. Latrophilin 1 and its endogenous ligand Lasso/teneurin-2 form a high-affinity transsynaptic receptor pair with signaling capabilities. Proc Natl Acad Sci U S A. 2011 Jul 19;108(29):12113-8. doi:, 10.1073/pnas.1019434108. Epub 2011 Jul 1. PMID:21724987 doi:https://dx.doi.org/10.1073/pnas.1019434108

[2] Silva JP, Lelianova VG, Ermolyuk YS, Vysokov N, Hitchen PG, Berninghausen O, Rahman MA, Zangrandi A, Fidalgo S, Tonevitsky AG, Dell A, Volynski KE, Ushkaryov YA. Latrophilin 1 and its endogenous ligand Lasso/teneurin-2 form a high-affinity transsynaptic receptor pair with signaling capabilities. Proc Natl Acad Sci U S A. 2011 Jul 19;108(29):12113-8. doi:, 10.1073/pnas.1019434108. Epub 2011 Jul 1. PMID:21724987 doi:https://dx.doi.org/10.1073/pnas.1019434108

[3] Li J, Shalev-Benami M, Sando R, Jiang X, Kibrom A, Wang J, Leon K, Katanski C, Nazarko O, Lu YC, Sudhof TC, Skiniotis G, Arac D. Structural Basis for Teneurin Function in Circuit-Wiring: A Toxin Motif at the Synapse. Cell. 2018 Apr 19;173(3):735-748.e15. doi: 10.1016/j.cell.2018.03.036. PMID:29677516 doi:https://dx.doi.org/10.1016/j.cell.2018.03.036

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@@ Line 3: / Line 3: @@
 <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 [http://en.wikipedia.org/wiki/Human Human]. 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 [http://proteopedia.org/fgij/fg.htm?mol=6CMX FirstGlance]. <br>
+<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='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></td></tr>
+</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TENM2, KIAA1127, ODZ2, TNM2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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'>[http://proteopedia.org/fgij/fg.htm?mol=6cmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cmx OCA], [http://pdbe.org/6cmx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cmx RCSB], [http://www.ebi.ac.uk/pdbsum/6cmx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cmx ProSAT]</span></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 ==
@@ Line 21: / Line 23: @@
 __TOC__
 </SX>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Arac, D]]
+[[Category: Arac D]]
-[[Category: Li, J]]
+[[Category: Li J]]
-[[Category: Shalev-Benami, M]]
+[[Category: Shalev-Benami M]]
-[[Category: Skiniotis, G]]
+[[Category: Skiniotis G]]
-[[Category: Sudhof, T]]
+[[Category: Sudhof T]]
-[[Category: Cn]]
-[[Category: Membrane protein]]
-[[Category: Teneurin]]

6cmx: Difference between revisions

Revision as of 07:52, 17 October 2024

Human Teneurin 2 extra-cellular region

Structural highlights

Function

Publication Abstract from PubMed

References

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Proteopedia Page Contributors and Editors (what is this?)

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