1kot

<StructureSection load='1kot' size='340' side='right'caption='[[1kot]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1kot]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KOT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KOT FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kot FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kot OCA], [https://pdbe.org/1kot PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kot RCSB], [https://www.ebi.ac.uk/pdbsum/1kot PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kot ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/GBRAP_HUMAN GBRAP_HUMAN]] May play a role in intracellular transport of GABA(A) receptors and its interaction with the cytoskeleton. Involved in apoptosis. Involved in autophagy (By similarity).<ref>PMID:15977068</ref>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:11875056</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1kot" style="background-color:#fffaf0;"></div>

[[Category: Human]]

[[Category: Luge, C]]

[[Category: Mayr, L M]]

[[Category: Stangler, T]]

[[Category: Willbold, D]]

[[Category: Transport protein]]