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Understanding insulin endocrinology in decapod Crustacea: molecular modelling characterization of an insulin-Binding Protein and insulin-like peptides in the eastern spiny lobster, Sagmariasus verreauxi

Citation

Chandler, JC and Gandhi, NS and Mancera, RL and Smith, G and Elizur, A and Ventura, T, Understanding insulin endocrinology in decapod Crustacea: molecular modelling characterization of an insulin-Binding Protein and insulin-like peptides in the eastern spiny lobster, Sagmariasus verreauxi, International Journal of Molecular Sciences, 18, (9) Article 1832. ISSN 1422-0067 (2017) [Refereed Article]


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Copyright Statement

Copyright 2017 The Authors. Licensed under Creative Commons Attribution 4.0 International (CC BY 4.0) https://creativecommons.org/licenses/by/4.0/

DOI: doi:10.3390/ijms18091832

Abstract

The insulin signalling system is one of the most conserved endocrine systems of Animalia from mollusc to man. In decapod Crustacea, such as the Eastern spiny lobster, Sagmariasus verreauxi (Sv) and the red-claw crayfish, Cherax quadricarinatus (Cq), insulin endocrinology governs male sexual differentiation through the action of a male-specific, insulin-like androgenic gland peptide (IAG). To understand the bioactivity of IAG it is necessary to consider its bio-regulators such as the insulin-like growth factor binding protein (IGFBP). This work has employed various molecular modelling approaches to represent S. verreauxi IGFBP and IAG, along with additional Sv-ILP ligands, in order to characterise their binding interactions. Firstly, we present Sv- and Cq-ILP2: neuroendocrine factors that share closest homology with Drosophila ILP8 (Dilp8). We then describe the binding interaction of the N-terminal domain of Sv-IGFBP and each ILP through a synergy of computational analyses. In-depth interaction mapping and computational alanine scanning of IGFBP_Ní highlight the conserved involvement of the hotspot residues Q67, G70, D71, S72, G91, G92, T93 and D94. The significance of the negatively charged residues D71 and D94 was then further exemplified by structural electrostatics. The functional importance of the negative surface charge of IGFBP is exemplified in the complementary electropositive charge on the reciprocal binding interface of all three ILP ligands. When examined, this electrostatic complementarity is the inverse of vertebrate homologues; such physicochemical divergences elucidate towards ligand-binding specificity between Phyla.

Item Details

Item Type:Refereed Article
Keywords:insulin endocrinology, decapod, Sagmariasus verreauxi, androgenic gland, molecular
Research Division:Agricultural and Veterinary Sciences
Research Group:Fisheries Sciences
Research Field:Aquaculture
Objective Division:Animal Production and Animal Primary Products
Objective Group:Fisheries - Aquaculture
Objective Field:Fisheries - Aquaculture not elsewhere classified
Author:Smith, G (Associate Professor Gregory Smith)
ID Code:120649
Year Published:2017
Funding Support:Australian Research Council (IH120100032)
Deposited By:Centre for Fisheries and Aquaculture
Deposited On:2017-08-30
Last Modified:2017-09-06
Downloads:17 View Download Statistics

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