1PQR

Solution Conformation of alphaA-Conotoxin EIVA

Summary for 1PQR

• Entry DOI: 10.2210/pdb1pqr/pdb
• NMR Information: BMRB: 5869
• Descriptor: Alpha-A-conotoxin EIVA (1 entity in total)
• Functional Keywords: alpha-helix, two disulfide bonds, c-term amidation, toxin
• Cellular location: Secreted: P58782
• Total number of polymer chains: 1
• Total formula weight: 3105.49

Authors

Chi, S.-W.,Park, K.-H.,Suk, J.-E.,Olivera, B.M.,McIntosh, J.M.,Han, K.-H. (deposition date: 2003-06-18, release date: 2003-11-04, Last modification date: 2022-03-02)

Primary citation

Chi, S.-W.,Park, K.-H.,Suk, J.-E.,Olivera, B.M.,McIntosh, J.M.,Han, K.-H.
Solution Conformation of alphaA-conotoxin EIVA, a Potent Neuromuscular Nicotinic Acetylcholine Receptor Antagonist from Conus ermineus
J.Biol.Chem., 278:42208-42213, 2003

PubMed Abstract: 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.

PubMed: 12900418
DOI: 10.1074/jbc.M303342200

Experimental method

SOLUTION NMR