1DG2
SOLUTION CONFORMATION OF A-CONOTOXIN AUIB
Summary for 1DG2
| Entry DOI | 10.2210/pdb1dg2/pdb |
| Descriptor | A-CONOTOXIN AUIB (1 entity in total) |
| Functional Keywords | a-helix, two disulfide bonds and c-term amidation, toxin |
| Biological source | Conus aulicus |
| Total number of polymer chains | 1 |
| Total formula weight | 1575.79 |
| Authors | Cho, J.-H.,Mok, K.H.,Olivera, B.M.,McIntosh, J.M.,Park, K.-H.,Han, K.-H. (deposition date: 1999-11-23, release date: 2000-02-25, Last modification date: 2022-02-16) |
| Primary citation | Cho, J.H.,Mok, K.H.,Olivera, B.M.,McIntosh, J.M.,Park, K.H.,Han, K.H. Nuclear magnetic resonance solution conformation of alpha-conotoxin AuIB, an alpha(3)beta(4) subtype-selective neuronal nicotinic acetylcholine receptor antagonist. J.Biol.Chem., 275:8680-8685, 2000 Cited by PubMed Abstract: The neuronal nicotinic acetylcholine receptors constitute a highly diverse group, with subtypes consisting of pentameric combinations of alpha and beta subunits. alpha-Conotoxins are a homologous series of small peptides that antagonize these receptors. We present the three-dimensional solution structure of alpha-conotoxin AuIB, the first 15-residue alpha-conotoxin known to selectively block the alpha(3)beta(4) nicotinic acetylcholine receptor subtype. The pairwise backbone and heavy-atom root mean square deviation for an ensemble of 20 structures are 0.269 and 0.720 A, respectively. The overall fold of alpha-conotoxin AuIB closely resembles that of the alpha4/7 subfamily alpha-conotoxins. However, the absence of Tyr(15), normally present in other alpha4/7 members, results in tight bending of the backbone at the C terminus and effectively renders Asp(14) to assume the spatial location of Tyr(15) present in other neuronal alpha4/7 alpha-conotoxins. Structural comparison of alpha-conotoxin AuIB with the alpha(3)beta(2) subtype-specific alpha-conotoxin MII shows different electrostatic surface charge distributions, which may be important in differential receptor subtype recognition. PubMed: 10722709DOI: 10.1074/jbc.275.12.8680 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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