Determination of a high-precision NMR structure of the minicollagen cysteine rich domain from Hydra and characterization of its disulfide bond formation

FEBS Letters
Sebastian MeierStephan Grzesiek

Abstract

A high-precision solution structure of the C-terminal minicollagen cysteine rich domain of Hydra has been determined using modern heteronuclear and weak alignment NMR techniques at natural isotope abundance. The domain consists of only 24 amino acids, six of which are prolines and six are cysteines bonded in disulfide bridges that constrain the structure into a new fold. The redox equilibrium of the structure has been characterized from a titration with glutathione. No local native structures are detectable in the reduced form. Thus, oxidation and folding are tightly coupled.

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Citations

Sep 16, 2008·Journal of the American Society for Mass Spectrometry·Liwen ZhangYeong-Renn Chen
Sep 12, 2014·Biotechnology Journal·Yun Jung YangHyung Joon Cha
Mar 18, 2015·Journal of Peptide Science : an Official Publication of the European Peptide Society·Sonja A Dames
Jan 24, 2007·Current Biology : CB·Sebastian MeierSuat Ozbek
Jan 22, 2008·Journal of Molecular Biology·Patrizia AdamczykSuat Ozbek
Feb 24, 2015·Molecular BioSystems·Seungjin NaJoseph Kwon
Oct 15, 2013·Journal of Computational Chemistry·Nandun M ThellamuregeHui Li
Jul 9, 2020·PloS One·Alfio Alessandro ChiarenzaDori L Contreras

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