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PDBsum entry 1kot
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Transport protein
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PDB id
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1kot
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Solution structure of human gaba(a) receptor-Associated protein gabarap: implications for biolgoical funcrion and its regulation.
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Authors
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T.Stangler,
L.M.Mayr,
D.Willbold.
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Ref.
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J Biol Chem, 2002,
277,
13363-13366.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 1.
Fig. 1. Solution structure of human GABARAP after
simulated annealing and refinement calculations. A, shown is the
superposition of the backbones of all 15 obtained structures. B,
ribbon presentation of the averaged GABARAP structure. Secondary
structure elements are labeled according to their sequential
arrangement. Amino- (N) and carboxyl (C)-terminal ends are
indicated. C, backbone worm presentation of GABARAP. Residues
that contain amide groups with split or broadened resonance
peaks are colored in red. Residues Val^6 and Asp^102 are also
colored in red because their amide resonances were undetectable.
This indicates that the respective residues are involved in
conformational exchange on a slow to intermediate time scale.
Prominent residues are labeled with amino acid type and sequence
position. All figures were prepared using MOLMOL (17).
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Figure 3.
Fig. 3. Focused view of the GABARAP structure. Shown is
the superposition of the backbone atom connections of residues
Met^1, Lys^2, Ala^36, Pro^37, Ala^108, and Tyr^115-Leu^117 (all
in black) for all obtained structures. The side chains of Met^1,
Ala^36, Pro^37, Ala^108, and Leu^117 (gray) form a hydrophobic
pocket for the side chain of Tyr^115 (blue). The hydroxyl oxygen
of the Tyr^115 phenolic ring is hydrogen-bonded to the backbone
amide nitrogen of Lys^2 (red).
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2002,
277,
13363-13366)
copyright 2002.
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