Open AccessSequence-specific backbone resonance assignments and microsecond timescale molecular dynamics simulation of human eosinophil-derived neurotoxin
Author(s) -
Donald Gagné,
C. S. Narayanan,
Khushboo Bafna,
Laurie-Anne Charest,
Pratul K. Agarwal,
Nicolas Doucet
Publication year - 2017
Publication title -
biomolecular nmr assignments
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.359
H-Index - 16
eISSN - 1874-2718
pISSN - 1874-270X
DOI - 10.1007/s12104-017-9736-9
Subject(s) - rnase p , ribonuclease , molecular dynamics , biology , microsecond , eosinophil cationic protein , biophysics , computational biology , rna , biochemistry , eosinophil , chemistry , physics , computational chemistry , immunology , gene , astronomy , asthma
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 the 1 H, 13 C and 15 N 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.