1kot
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(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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Revision as of 15:46, 12 November 2007
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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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