6CMX
Human Teneurin 2 extra-cellular region
Summary for 6CMX
Entry DOI | 10.2210/pdb6cmx/pdb |
EMDB information | 7526 |
Related PRD ID | PRD_900118 |
Descriptor | Teneurin-2, alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose, ... (5 entities in total) |
Functional Keywords | teneurin, membrane protein, cns |
Biological source | Homo sapiens (Human) |
Total number of polymer chains | 1 |
Total formula weight | 227465.99 |
Authors | Shalev-Benami, M.,Li, J.,Sudhof, T.,Skiniotis, G.,Arac, D. (deposition date: 2018-03-06, release date: 2018-07-25, Last modification date: 2025-06-04) |
Primary citation | Li, J.,Shalev-Benami, M.,Sando, R.,Jiang, X.,Kibrom, A.,Wang, J.,Leon, K.,Katanski, C.,Nazarko, O.,Lu, Y.C.,Sudhof, T.C.,Skiniotis, G.,Arac, D. Structural Basis for Teneurin Function in Circuit-Wiring: A Toxin Motif at the Synapse. Cell, 173:735-748.e15, 2018 Cited by PubMed Abstract: Teneurins (TENs) are cell-surface adhesion proteins with critical roles in tissue development and axon guidance. Here, we report the 3.1-Å cryoelectron microscopy structure of the human TEN2 extracellular region (ECR), revealing a striking similarity to bacterial Tc-toxins. The ECR includes a large β 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 β propeller is attached in a perpendicular orientation. We further show that an alternatively spliced region within the β 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. PubMed: 29677516DOI: 10.1016/j.cell.2018.03.036 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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