1pqr
From Proteopedia
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Solution Conformation of alphaA-Conotoxin EIVA
Overview
We report the solution three-dimensional structure of an alphaA-conotoxin, EIVA determined by nuclear magnetic resonance spectroscopy and restrained, molecular dynamics. The alphaA-conotoxin EIVA consists of 30 amino acids, representing the largest peptide among the alpha/alphaA-family conotoxins, discovered so far and targets the neuromuscular nicotinic acetylcholine, receptor with high affinity. alphaA-Conotoxin EIVA consists of three, distinct structural domains. The first domain is mainly composed of the, Cys3-Cys11-disulfide loop and is structurally ill-defined with a large, backbone root mean square deviation of 1.91 A. The second domain formed by, residues His12-Hyp21 is extremely well defined with a backbone root mean, square deviation of 0.52 A, thus forming a sturdy stem for the entire, molecule. The third C-terminal domain formed by residues Hyp22-Gly29 shows, an intermediate structural order having a backbone root mean square, deviation of 1.04 A. A structurally ill-defined N-terminal first loop, domain connected to a rigid central molecular stem seems to be the general, structural feature of the alphaA-conotoxin subfamily. A detailed, structural comparison between alphaA-conotoxin EIVA and alphaA-conotoxin, PIVA suggests that the higher receptor affinity of alphaA-conotoxin EIVA, than alphaA-conotoxin PIVA might originate from different steric, disposition and charge distribution in the second loop "handle" motif.
About this Structure
1PQR is a Single protein structure of sequence from [1] with NH2 as ligand. Full crystallographic information is available from OCA.
Reference
Solution conformation of alphaA-conotoxin EIVA, a potent neuromuscular nicotinic acetylcholine receptor antagonist from Conus ermineus., Chi SW, Park KH, Suk JE, Olivera BM, McIntosh JM, Han KH, J Biol Chem. 2003 Oct 24;278(43):42208-13. Epub 2003 Aug 4. PMID:12900418
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