Journal article
Solution structure, aggregation behavior, and flexibility of human relaxin-2
LM Haugaard-Kedstro M., MA Hossain, NL Daly, RAD Bathgate, E Rinderknecht, JD Wade, DJ Craik, KJ Rosengren
ACS Chemical Biology | Published : 2015
DOI: 10.1021/cb500918v
Abstract
Relaxin is a member of the relaxin/insulin peptide hormone superfamily and is characterized by a two-chain structure constrained by three disulfide bonds. Relaxin is a pleiotropic hormone and involved in a number of physiological and pathogenic processes, including collagen and cardiovascular regulation and tissue remodelling during pregnancy and cancer. Crystallographic and ultracentrifugation experiments have revealed that the human form of relaxin, H2 relaxin, self-associates into dimers, but the significance of this is poorly understood. Here, we present the NMR structure of a monomeric, amidated form of H2 relaxin and compare its features and behavior in solution to those of native H2 r..
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Grants
Awarded by National Health and Medical Research Council
Funding Acknowledgements
We gratefully acknowledge the use of the Queensland NMR Network 900 MHz spectrometer. L.M.H.K. is a recipient of a Swedish Research Council Post-Doctoral Fellowship. N.L.D. and K.J.R. are Australian Research Council (ARC) Future Fellows. R.A.D.B. is a National and Medical Health Research Council (NHMRC, Australia) Senior Research Fellow. J.D.W. is an NHMRC Principal Research Fellow. D.J.C. is an NHMRC Senior Principal Research Fellow. This work was supported by the Faculty of Natural Sciences and Technology, Linnaeus University (K.J.R.) and by NHMRC Project grants 1023078 (J.D.W., R.A.D.B. M.A.H.) and 1043750 (R.A.D.B., K.J.R.).