Identification of hydrophobic interactions between relaxin-3 and its receptor RXFP3: implication for a conformational change in the B-chain C-terminus during receptor binding-Reference-Cited by-同舟云学术

Identification of hydrophobic interactions between relaxin-3 and its receptor RXFP3: implication for a conformational change in the B-chain C-terminus during receptor binding

Published:2016-05-19 Issue:9 Volume:48 Page:2227-2236
ISSN:0939-4451
Container-title:Amino Acids
language:en
Short-container-title:Amino Acids

Author:

Hu Meng-Jun,Shao Xiao-Xia,Wang Jia-Hui,Wei Dian,Liu Ya-Li,Xu Zeng-Guang,Guo Zhan-Yun

Funder

National Natural Science Foundation of China

Publisher

Springer Science and Business Media LLC

Subject

Organic Chemistry,Clinical Biochemistry,Biochemistry

Link

http://link.springer.com/content/pdf/10.1007/s00726-016-2260-x.pdf

Reference29 articles.

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2. Bathgate RA, Oh MH, Ling WJ, Kaas Q, Hossain MA, Gooley PR, Rosengren KJ (2013) Elucidation of relaxin-3 binding interactions in the extracellular loops of RXFP3. Front Endocrinol (Lausanne) 4:13

3. Haugaard-Jönsson LM, Hossain MA, Daly NL, Craik DJ, Wade JD, Rosengren KJ (2009) Structure of human insulin-like peptide 5 and characterization of conserved hydrogen bonds and electrostatic interactions within the relaxin framework. Biochem J 419:619–627

4. Haugaard-Kedström LM, Hossain MA, Daly NL, Bathgate RA, Rinderknecht E, Wade JD, Craik DJ, Rosengren KJ (2015) Solution structure, aggregation behavior, and flexibility of human relaxin-2. ACS Chem Biol 10:891–900

5. Hosken IT, Sutton SW, Smith CM, Gundlach AL (2015) Relaxin-3 receptor (RXFP3) gene knockout mice display reduced running wheel activity: implications for role of relaxin-3/RXFP3 signalling in sustained arousal. Behav Brain Res 278:167–175

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