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

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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University of Melbourne Researchers

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.).