Journal article icon

Journal article

Structural basis of Latrophilin-FLRT interaction

Abstract:

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...

Expand abstract
Publication status:
Published
Peer review status:
Peer reviewed

Actions


Access Document


Files:
Publisher copy:
10.1016/j.str.2015.01.013

Authors


More by this author
Department:
Biochemistry
Role:
Author
More by this author
Department:
Biochemistry
Role:
Author
More by this author
Department:
Biochemistry
Role:
Author
More by this author
Department:
Structural Biology
Role:
Author
Expand authors...
More from this funder
Grant:
MR/ L018039/1
Funding agency for:
Project
More from this funder
Funding agency for:
Project
More from this funder
Grant:
SFB 834; EXC 115
Funding agency for:
Project
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:
1878-4186
ISSN:
0969-2126
Language:
English

Terms of use


Metrics



If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP