PDBsum entry 1kot

Transport protein

PDB id: 1kot

Contents

Protein chain

119 a.a. *

* Residue conservation analysis

PDB id:

1kot

Name:

Transport protein

Title:

Solution structure of human gaba receptor associated protein gabarap

Structure:

Gabarap. Chain: a. Synonym: gaba-a receptor-associated protein. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

NMR struc:

15 models

Authors:

T.Stangler,C.Luge,L.M.Mayr,D.Willbold

Key ref:

T.Stangler et al. (2002). Solution structure of human GABA(A) receptor-associated protein GABARAP: implications for biolgoical funcrion and its regulation. J Biol Chem, 277, 13363-13366. PubMed id: 11875056 DOI: 10.1074/jbc.C200050200

Date:

22-Dec-01 Release date: 16-Jan-02

Protein chain

O95166  (GBRAP_HUMAN) -  Gamma-aminobutyric acid receptor-associated protein from Homo sapiens

Seq: 117 a.a.

Struc: 119 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1074/jbc.C200050200

J Biol Chem 277:13363-13366 (2002)

PubMed id: 11875056

Solution structure of human GABA(A) receptor-associated protein GABARAP: implications for biolgoical funcrion and its regulation.

T.Stangler, L.M.Mayr, D.Willbold.

ABSTRACT

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.

Selected figure(s)

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).

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).

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2002, 277, 13363-13366) copyright 2002.

Figures were selected by an automated process.