Solution structure, aggregation behavior, and flexibility of human relaxin-2

Haugaard-Kedstrom, Linda, Hossain, Mohammed Akhter, Daly, Norelle L., Bathgate, Ross A. D., Rinderknecht, Ernst, Wade, John D., Craik, David J. and Rosengren, Karl Johan (2015) Solution structure, aggregation behavior, and flexibility of human relaxin-2. ACS Chemical Biology, 10 3: 891-900. doi:10.1021/cb500918v

Author Haugaard-Kedstrom, Linda
Hossain, Mohammed Akhter
Daly, Norelle L.
Bathgate, Ross A. D.
Rinderknecht, Ernst
Wade, John D.
Craik, David J.
Rosengren, Karl Johan
Title Solution structure, aggregation behavior, and flexibility of human relaxin-2
Journal name ACS Chemical Biology   Check publisher's open access policy
ISSN 1554-8937
Publication date 2015-03-20
Year available 2015
Sub-type Article (original research)
DOI 10.1021/cb500918v
Open Access Status
Volume 10
Issue 3
Start page 891
End page 900
Total pages 10
Place of publication Washington, DC United States
Publisher American Chemical Society
Collection year 2016
Language eng
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 relaxin. The overall structure of H2 relaxin is retained in the monomeric form. H2 relaxin amide is fully active at the relaxin receptor RXFP1 and thus dimerization is not required for biological activity. Analysis of NMR chemical shifts and relaxation parameters identified internal motion in H2 relaxin at the pico-nanosecond and milli-microsecond time scales, which is commonly seen in other relaxin and insulin peptides and might be related to function.
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2016 Collection
School of Biomedical Sciences Publications
Institute for Molecular Bioscience - Publications
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Citation counts: TR Web of Science Citation Count  Cited 7 times in Thomson Reuters Web of Science Article | Citations
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Created: Thu, 26 Mar 2015, 14:43:06 EST by Susan Allen on behalf of Institute for Molecular Bioscience