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  Crystal structure of the GABA(A)-receptor-associated protein, GABARAP

Bavro, V. N., Sola, M., Bracher, A., Kneussel, M., Betz, H., & Weissenhorn, W. (2002). Crystal structure of the GABA(A)-receptor-associated protein, GABARAP. EMBO Reports, 3(2), 183-189.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-1FC1-9 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-1FC2-7
Genre: Journal Article

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Bavro, V. N., Author
Sola, M., Author
Bracher, A., Author
Kneussel, M.1, Author              
Betz, H.1, Author              
Weissenhorn, W., Author
Affiliations:
1Neurochemistry Department, Max Planck Institute for Brain Research, Max Planck Society, ou_2461704              

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 Abstract: The GABA(A)-receptor-associated protein (GABARAP) is a member of a growing family of intracellular membrane trafficking and/or fusion proteins and has been implicated in plasma membrane targeting and/or recycling of GABA(A) receptors. GABARAP is localized on intracellular membranes such as the trans-Golgi network, binds to the 72 subunit of GABAA receptors and interacts with microtubules and the N-ethylmaleimide- sensitive factor. We report the X-ray crystal structure of mammalian GABARAP at 2.0 Angstrom resolution. GABARAP consists of an N-terminal basic helical region, which has been implicated in tubulin binding, and a core structure with a conserved ubiquitin-like fold. Consistent with the high extent of sequence conservation among GABARAP homologues from plants to mammals, one face of the core structure is absolutely conserved while the opposite face shows considerable divergence. These features are in agreement with the conserved surface mediating protein-protein interactions shared by all members of the family, whereas the non-conserved surface region may play specific roles, such as docking to particular membrane receptors.

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Language(s): eng - English
 Dates: 2002
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: eDoc: 10480
ISI: 000174156100018
 Degree: -

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Title: EMBO Reports
  Alternative Title : EMBO Rep.
Source Genre: Journal
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Pages: - Volume / Issue: 3 (2) Sequence Number: - Start / End Page: 183 - 189 Identifier: ISSN: 1469-221X