title: Sequence-specific backbone resonance assignments and microsecond timescale molecular dynamics simulation of human eosinophil-derived neurotoxin.
abstract: Eight active canonical members of the pancreatic-like ribonuclease A (RNase A) superfamily have been identified in human. All structural homologs share similar RNA-degrading functions, while also cumulating other various biological activities in different tissues. The functional homologs eosinophil-derived neurotoxin (EDN, or RNase 2) and eosinophil cationic protein (ECP, or RNase 3) are known to be expressed and secreted by eosinophils in response to infection, and have thus been postulated to play an important role in host defense and inflammatory response. We recently initiated the biophysical and dynamical investigation of several vertebrate RNase homologs and observed that clustering residue dynamics appear to be linked with the phylogeny and biological specificity of several members. Here we report the1H,13C and15N backbone resonance assignments of human EDN (RNase 2) and its molecular dynamics simulation on the microsecond timescale, providing means to pursue this comparative atomic-scale functional and dynamical analysis by NMR and computation over multiple time frames.
authors.affiliation: INRS-Institut Armand-Frappier, Université du Québec, 531 Boulevard des Prairies, Laval, QC, H7V 1B7, Canada.|Structural Biology Initiative, CUNY Advanced Science Research Center, New York, NY, 10031, USA.
authors.forename: Donald
authors.initials: D
authors.lastname: Gagné
authors.affiliation: INRS-Institut Armand-Frappier, Université du Québec, 531 Boulevard des Prairies, Laval, QC, H7V 1B7, Canada.
authors.forename: Chitra
authors.initials: C
authors.lastname: Narayanan
authors.affiliation: Graduate School of Genome Science and Technology, University of Tennessee, Knoxville, TN, 37996, USA.
authors.forename: Khushboo
authors.initials: K
authors.lastname: Bafna
authors.affiliation: INRS-Institut Armand-Frappier, Université du Québec, 531 Boulevard des Prairies, Laval, QC, H7V 1B7, Canada.
authors.forename: Laurie-Anne
authors.initials: LA
authors.lastname: Charest
authors.affiliation: Computational Biology Institute and Computer Science and Mathematics Division, Oak Ridge National Laboratory, 1 Bethel Valley Road, Oak Ridge, TN, 37830, USA.|Department of Biochemistry, Cellular and Molecular Biology, University of Tennessee, Knoxville, TN, 37996, USA.
authors.forename: Pratul K
authors.initials: PK
authors.lastname: Agarwal
authors.affiliation: INRS-Institut Armand-Frappier, Université du Québec, 531 Boulevard des Prairies, Laval, QC, H7V 1B7, Canada. nicolas.doucet@iaf.inrs.ca.|PROTEO, The Québec Network for Research on Protein Function, Engineering, and Applications, Université Laval, 1045 Avenue de la Médecine, Quebec, QC, G1V 0A6, Canada. nicolas.doucet@iaf.inrs.ca.|GRASP, The Groupe de recherche Axé sur la Structure des Protéines, McGill University, 3649 Promenade Sir William Osler, Montreal, QC, H3G 0B1, Canada. nicolas.doucet@iaf.inrs.ca.
authors.forename: Nicolas
authors.identifier: http://orcid.org/0000-0002-1952-9380
authors.initials: N
authors.lastname: Doucet
mesh_terms: D000595:Amino Acid Sequence; D047208:Eosinophil-Derived Neurotoxin / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D056004:Molecular Dynamics Simulation; D019906:Nuclear Magnetic Resonance, Biomolecular; D000072417:Protein Domains; D013997:Time Factors
chemical_list: D047208:Eosinophil-Derived Neurotoxin
keywords: EDN; Enzyme dynamics; Protein orthologs; RNA; RNase 2; RNase A; Ribonucleases