1kot
From Proteopedia
(New page: 200px<br /> <applet load="1kot" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kot" /> '''Solution Structure of Human GABA Receptor A...) |
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'''Solution Structure of Human GABA Receptor Associated Protein GABARAP'''<br /> | '''Solution Structure of Human GABA Receptor Associated Protein GABARAP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Control of neurotransmitter receptor expression and delivery to the | + | Control of neurotransmitter receptor expression and delivery to the postsynaptic membrane is of critical importance for neural signal transduction at synapses. The gamma-aminobutyric acid, type A (GABA(A)) receptor-associated protein GABARAP was reported to have an important role for movement and sorting of GABA(A) receptor molecules to the postsynaptic membrane. GABARAP not only binds to GABA(A) receptor gamma2-subunit but also to tubulin, gephyrin, and ULK1. We present for the first time the high resolution structure of human GABARAP determined by nuclear magnetic resonance in aqueous solution. One part of the molecule, despite being well ordered and rigid on a MHz time scale, exists in at least two different conformations that interchange with each other on a time scale slower than 25 Hz. An important feature of the solution structure is the observation that amino- and carboxyl-terminal ends of the protein directly interact with each other, which is not seen in recently reported crystal structures. The possible biological relevance of these observations for the regulation of GABARAP interactions and functions is discussed. |
==About this Structure== | ==About this Structure== | ||
| - | 1KOT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1KOT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KOT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Luge, C.]] | [[Category: Luge, C.]] | ||
| - | [[Category: Mayr, L | + | [[Category: Mayr, L M.]] |
[[Category: Stangler, T.]] | [[Category: Stangler, T.]] | ||
[[Category: Willbold, D.]] | [[Category: Willbold, D.]] | ||
[[Category: human gaba receptor targeting gabarap]] | [[Category: human gaba receptor targeting gabarap]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:36:24 2008'' |
Revision as of 11:36, 21 February 2008
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Solution Structure of Human GABA Receptor Associated Protein GABARAP
Overview
Control of neurotransmitter receptor expression and delivery to the postsynaptic membrane is of critical importance for neural signal transduction at synapses. The gamma-aminobutyric acid, type A (GABA(A)) receptor-associated protein GABARAP was reported to have an important role for movement and sorting of GABA(A) receptor molecules to the postsynaptic membrane. GABARAP not only binds to GABA(A) receptor gamma2-subunit but also to tubulin, gephyrin, and ULK1. We present for the first time the high resolution structure of human GABARAP determined by nuclear magnetic resonance in aqueous solution. One part of the molecule, despite being well ordered and rigid on a MHz time scale, exists in at least two different conformations that interchange with each other on a time scale slower than 25 Hz. An important feature of the solution structure is the observation that amino- and carboxyl-terminal ends of the protein directly interact with each other, which is not seen in recently reported crystal structures. The possible biological relevance of these observations for the regulation of GABARAP interactions and functions is discussed.
About this Structure
1KOT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of human GABA(A) receptor-associated protein GABARAP: implications for biolgoical funcrion and its regulation., Stangler T, Mayr LM, Willbold D, J Biol Chem. 2002 Apr 19;277(16):13363-6. Epub 2002 Mar 1. PMID:11875056
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