Journal article
Structural basis of Latrophilin-FLRT interaction
- Abstract:
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Latrophilins, receptors for spider venom α-latrotoxin, are adhesion type G-protein-coupled receptors with emerging functions in synapse development. The N-terminal region binds the endogenous cell adhesion molecule FLRT, a major regulator of cortical and synapse development. We present crystallographic data for the mouse Latrophilin3 lectin and olfactomedin-like (Olf) domains, thereby revealing the Olf β-propeller fold and conserved calcium-binding site. We locate the FLRT-Latrophilin binding...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(pdf, 2.6MB)
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- Publisher copy:
- 10.1016/j.str.2015.01.013
- Publication website:
- http://www.cell.com/structure/abstract/S0969-2126%2815%2900037-4
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Authors
Funding
Max-Planck Society
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Bibliographic Details
- Publisher:
- Elsevier Publisher's website
- Journal:
- Structure
- Volume:
- 23
- Issue:
- 4
- Pages:
- 774-781
- Publication date:
- 2015-02-26
- Acceptance date:
- 2015-01-19
- DOI:
- EISSN:
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1878-4186
- ISSN:
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0969-2126
Item Description
- Language:
- English
- UUID:
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uuid:2ad757fe-e0b1-4ce8-81ba-777ae1b567d6
- Deposit date:
- 2015-05-27
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