Journal article
Structure of human insulin-like peptide 5 and characterization of conserved hydrogen bonds and electrostatic interactions within the relaxin framework
LM Haugaard-Jönsson, MA Hossain, NL Daly, DJ Craik, JD Wade, KJ Rosengren
Biochemical Journal | PORTLAND PRESS LTD | Published : 2009
DOI: 10.1042/BJ20082353
Abstract
INSL5 (insulin-like peptide 5) is a two-chain peptide hormone related to insulin and relaxin. It was recently discovered through searches of expressed sequence tag databases and, although the full biological significance of INSL5 is still being elucidated, high expression in peripheral tissues such as the colon, as well as in the brain and hypothalamus, suggests roles in gut contractility and neuroendocrine signalling. INSL5 activates the relaxin family peptide receptor 4 with high potency and appears to be the endogenous ligand for this receptor, on the basis of overlapping expression profiles and their apparent co-evolution. In the present study, we have used solution-state NMR to characte..
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Awarded by National Health and Medical Research Council, Australia
Funding Acknowledgements
K. J. R. receives financial support from the Faculty of Natural Sciences and Technology, University of Kalmar and Ake Wiberg's Foundation. J. D.W. is supported by the National Health and Medical Research Council, Australia [project grant number 508995]. D. J. C. is a National Health and Medical Research Council Principal Research Fellow. N. L. D. is a Queensland Smart State Fellow.