6fb3

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(Difference between revisions)

Current revision

Teneurin 2 Partial Extracellular Domain

Structural highlights

6fb3 is a 4 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.38Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TEN2_CHICK Acts as a ligand of the ADGRL1 receptor (By similarity). 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. May also mediates axon guidance and heterophilic cell-cell adhesion. May function as a cellular signal transducer.^[1] ^[2] ^[3] Ten-2 intracellular domain: Induces gene transcription inhibition.

Publication Abstract from PubMed

Teneurins are ancient cell-cell adhesion receptors that are vital for brain development and synapse organisation. They originated in early metazoan evolution through a horizontal gene transfer event when a bacterial YD-repeat toxin fused to a eukaryotic receptor. We present X-ray crystallography and cryo-EM structures of two Teneurins, revealing a ~200 kDa extracellular super-fold in which eight sub-domains form an intricate structure centred on a spiralling YD-repeat shell. An alternatively spliced loop, which is implicated in homophilic Teneurin interaction and specificity, is exposed and thus poised for interaction. The N-terminal side of the shell is 'plugged' via a fibronectin-plug domain combination, which defines a new class of YD proteins. Unexpectedly, we find that these proteins are widespread amongst modern bacteria, suggesting early metazoan receptor evolution from a distinct class of proteins, which today includes both bacterial proteins and eukaryotic Teneurins.

Structures of Teneurin adhesion receptors reveal an ancient fold for cell-cell interaction.,Jackson VA, Meijer DH, Carrasquero M, van Bezouwen LS, Lowe ED, Kleanthous C, Janssen BJC, Seiradake E Nat Commun. 2018 Mar 14;9(1):1079. doi: 10.1038/s41467-018-03460-0. PMID:29540701^[4]

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

References

↑ Rubin BP, Tucker RP, Martin D, Chiquet-Ehrismann R. Teneurins: a novel family of neuronal cell surface proteins in vertebrates, homologous to the Drosophila pair-rule gene product Ten-m. Dev Biol. 1999 Dec 1;216(1):195-209. PMID:10588872 doi:http://dx.doi.org/10.1006/dbio.1999.9503
↑ Rubin BP, Tucker RP, Brown-Luedi M, Martin D, Chiquet-Ehrismann R. Teneurin 2 is expressed by the neurons of the thalamofugal visual system in situ and promotes homophilic cell-cell adhesion in vitro. Development. 2002 Oct;129(20):4697-705. PMID:12361962
↑ Bagutti C, Forro G, Ferralli J, Rubin B, Chiquet-Ehrismann R. The intracellular domain of teneurin-2 has a nuclear function and represses zic-1-mediated transcription. J Cell Sci. 2003 Jul 15;116(Pt 14):2957-66. doi: 10.1242/jcs.00603. Epub 2003 Jun, 3. PMID:12783990 doi:http://dx.doi.org/10.1242/jcs.00603
↑ Jackson VA, Meijer DH, Carrasquero M, van Bezouwen LS, Lowe ED, Kleanthous C, Janssen BJC, Seiradake E. Structures of Teneurin adhesion receptors reveal an ancient fold for cell-cell interaction. Nat Commun. 2018 Mar 14;9(1):1079. doi: 10.1038/s41467-018-03460-0. PMID:29540701 doi:http://dx.doi.org/10.1038/s41467-018-03460-0

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6fb3"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6fb3 is ON HOLD
+==Teneurin 2 Partial Extracellular Domain==
+<StructureSection load='6fb3' size='340' side='right'caption='[[6fb3]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6fb3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FB3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FB3 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.38&#8491;</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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=6fb3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fb3 OCA], [https://pdbe.org/6fb3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fb3 RCSB], [https://www.ebi.ac.uk/pdbsum/6fb3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fb3 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TEN2_CHICK TEN2_CHICK] Acts as a ligand of the ADGRL1 receptor (By similarity). 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. May also mediates axon guidance and heterophilic cell-cell adhesion. May function as a cellular signal transducer.<ref>PMID:10588872</ref> <ref>PMID:12361962</ref> <ref>PMID:12783990</ref>   Ten-2 intracellular domain: Induces gene transcription inhibition.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Teneurins are ancient cell-cell adhesion receptors that are vital for brain development and synapse organisation. They originated in early metazoan evolution through a horizontal gene transfer event when a bacterial YD-repeat toxin fused to a eukaryotic receptor. We present X-ray crystallography and cryo-EM structures of two Teneurins, revealing a ~200 kDa extracellular super-fold in which eight sub-domains form an intricate structure centred on a spiralling YD-repeat shell. An alternatively spliced loop, which is implicated in homophilic Teneurin interaction and specificity, is exposed and thus poised for interaction. The N-terminal side of the shell is 'plugged' via a fibronectin-plug domain combination, which defines a new class of YD proteins. Unexpectedly, we find that these proteins are widespread amongst modern bacteria, suggesting early metazoan receptor evolution from a distinct class of proteins, which today includes both bacterial proteins and eukaryotic Teneurins.
-Authors:
+Structures of Teneurin adhesion receptors reveal an ancient fold for cell-cell interaction.,Jackson VA, Meijer DH, Carrasquero M, van Bezouwen LS, Lowe ED, Kleanthous C, Janssen BJC, Seiradake E Nat Commun. 2018 Mar 14;9(1):1079. doi: 10.1038/s41467-018-03460-0. PMID:29540701<ref>PMID:29540701</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 6fb3" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Gallus gallus]]
+[[Category: Large Structures]]
+[[Category: Carrasquero M]]
+[[Category: Jackson VA]]
+[[Category: Lowe ED]]
+[[Category: Seiradake E]]

6fb3

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Current revision

Teneurin 2 Partial Extracellular Domain

Structural highlights

Function

Publication Abstract from PubMed

References

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