7bam

<table><tr><td colspan='2'>[[7bam]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BAM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BAM FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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"><div style='overflow: auto; max-height: 3em;'>[[7ban|7ban]], [[7bao|7bao]]</div></td></tr>

== Disease ==

[[https://www.uniprot.org/uniprot/TEN4_HUMAN TEN4_HUMAN]] NON RARE IN EUROPE: Hereditary essential tremor. The disease is caused by variants affecting the gene represented in this entry.

== Function ==

[[https://www.uniprot.org/uniprot/TEN4_HUMAN TEN4_HUMAN]] Involved in neural development, regulating the establishment of proper connectivity within the nervous system. Plays a role in the establishment of the anterior-posterior axis during gastrulation. Regulates the differentiation and cellular process formation of oligodendrocytes and myelination of small-diameter axons in the central nervous system (CNS) (PubMed:26188006). Promotes activation of focal adhesion kinase. May function as a cellular signal transducer (By similarity).[UniProtKB:Q3UHK6]<ref>PMID:26188006</ref>

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== Publication Abstract from PubMed ==

Establishment of correct synaptic connections is a crucial step during neural circuitry formation. The Teneurin family of neuronal transmembrane proteins promotes cell-cell adhesion via homophilic and heterophilic interactions, and is required for synaptic partner matching in the visual and hippocampal systems in vertebrates. It remains unclear how individual Teneurins form macromolecular cis- and trans-synaptic protein complexes. Here, we present a 2.7 A cryo-EM structure of the dimeric ectodomain of human Teneurin4. The structure reveals a compact conformation of the dimer, stabilized by interactions mediated by the C-rich, YD-shell, and ABD domains. A 1.5 A crystal structure of the C-rich domain shows three conserved calcium binding sites, and thermal unfolding assays and SAXS-based rigid-body modeling demonstrate that the compactness and stability of Teneurin4 dimers are calcium-dependent. Teneurin4 dimers form a more extended conformation in conditions that lack calcium. Cellular assays reveal that the compact cis-dimer is compatible with homomeric trans-interactions. Together, these findings support a role for teneurins as a scaffold for macromolecular complex assembly and the establishment of cis- and trans-synaptic interactions to construct functional neuronal circuits.

Teneurin4 dimer structures reveal a calcium-stabilized compact conformation supporting homomeric trans-interactions.,Meijer DH, Frias CP, Beugelink JW, Deurloo YN, Janssen BJC EMBO J. 2022 Jan 31:e107505. doi: 10.15252/embj.2020107505. PMID:35099835<ref>PMID:35099835</ref>

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

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<div class="pdbe-citations 7bam" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Janssen, B J.C]]

[[Category: Meijer, D H]]

[[Category: Synaptic cell adhesion]]