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Journal article

Structural basis of dynamic glycine receptor clustering by gephyrin.

Abstract:

Gephyrin is a bi-functional modular protein involved in molybdenum cofactor biosynthesis and in postsynaptic clustering of inhibitory glycine receptors (GlyRs). Here, we show that full-length gephyrin is a trimer and that its proteolysis in vitro causes the spontaneous dimerization of its C-terminal region (gephyrin-E), which binds a GlyR beta-subunit-derived peptide with high and low affinity. The crystal structure of the tetra-domain gephyrin-E in complex with the beta-peptide bound to doma...

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Publication status:
Published

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Publisher copy:
10.1038/sj.emboj.7600256

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Institution:
University of Oxford
Department:
Oxford, MPLS, Physics
Role:
Author
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Journal:
The EMBO journal
Volume:
23
Issue:
13
Pages:
2510-2519
Publication date:
2004-07-05
DOI:
EISSN:
1460-2075
ISSN:
0261-4189
URN:
uuid:e7048873-4000-406a-b074-82cfda61c7fa
Source identifiers:
154249
Local pid:
pubs:154249

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