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The Native Conformation of the Human VDAC1 N Terminus
Author(s) -
Schneider Robert,
Etzkorn Manuel,
Giller Karin,
Daebel Venita,
Eisfeld Jörg,
Zweckstetter Markus,
Griesinger Christian,
Becker Stefan,
Lange Adam
Publication year - 2010
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200906241
Subject(s) - barrel (horology) , voltage dependent anion channel , nuclear magnetic resonance spectroscopy , chemistry , vdac1 , c terminus , n terminus , crystallography , biophysics , conformational change , solid state nuclear magnetic resonance , lipid bilayer , stereochemistry , biochemistry , peptide sequence , materials science , amino acid , physics , biology , membrane , bacterial outer membrane , nuclear magnetic resonance , escherichia coli , composite material , gene
Roll out the barrel : The conformation of the N‐terminal domain of a functional human voltage‐dependent anion channel (hVDAC1) in lipid bilayers has been determined (see picture; overlay of NMR model (blue) and X‐ray structure (red/gray)). Solid‐state NMR spectroscopy reveals that the N terminus assumes a well‐defined, rigid structure and that its removal induces a conformational change in the hVDAC1 β‐barrel.
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