1DXZ
M2 TRANSMEMBRANE SEGMENT OF ALPHA-SUBUNIT OF NICOTINIC ACETYLCHOLINE RECEPTOR FROM TORPEDO CALIFORNICA, NMR, 20 STRUCTURES
Summary for 1DXZ
| Entry DOI | 10.2210/pdb1dxz/pdb |
| Related | 1ABT 1TOR 1TOS |
| Descriptor | ACETYLCHOLINE RECEPTOR PROTEIN, ALPHA CHAIN (1 entity in total) |
| Functional Keywords | transmembrane protein, nicotinic acetylcholine receptor, transmembrane segment, m2, ion-channel |
| Biological source | TORPEDO CALIFORNICA (PACIFIC ELECTRIC RAY) |
| Cellular location | Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein: P02710 |
| Total number of polymer chains | 1 |
| Total formula weight | 3416.07 |
| Authors | Pashkov, V.S.,Maslennikov, I.V.,Tchikin, L.D.,Efremov, R.G.,Ivanov, V.T.,Arseniev, A.S. (deposition date: 2000-01-20, release date: 2000-02-02, Last modification date: 2024-11-13) |
| Primary citation | Pashkov, V.S.,Maslennikov, I.V.,Tchikin, L.D.,Efremov, R.G.,Ivanov, V.T.,Arseniev, A.S. Spatial Structure of the M2 Transmembrane Segment of the Nicotinic Acetylcholine Receptor Alpha-Subunit FEBS Lett., 457:117-, 1999 Cited by PubMed Abstract: A synthetic peptide corresponding to the transmembrane segment M2 (residues 236-267) of the alpha-subunit of the nicotinic acetylcholine receptor from Torpedo californica has been studied by two dimensional 1H-NMR spectroscopy in a chloroform-methanol (1:1) mixture containing 0.1 M LiClO4. Reconstruction of the spatial structure of M2 from the NMR data resulted in an alpha-helix formed by residues 241-263. Distribution of the molecular hydrophobicity potential on the helix surface is very similar to that in five-helix bundles of proteins with a known three dimensional structure: two hydrophilic bands located on the opposite helix sides separated by strong hydrophobic zones. PubMed: 10486576DOI: 10.1016/S0014-5793(99)01023-6 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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