Journal of Integrative Natural Science (통합자연과학논문집)

The Basic Science Institute Chosun University (조선대학교 기초과학연구원)
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Three-Dimensional Structure Prediction of Follicle-Stimulating Hormone Receptor Transmembrane Domain by Homology Modelling

  • Priya dharshini B (Department of Medical Genetics, Chettinad Hospital and Research institute)
  • Received : 2023.02.28
  • Accepted : 2023.03.21
  • Published : 2023.04.10
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Abstract

The follicle stimulating hormone receptor (FSHR) is a glycoprotein hormone, that belongs to the GPCR superfamily. FSHR plays a major role in reproduction. The aberrant activation of FHS receptor leads to infertility and several reproductive disorders. The recently recognized roles of the FSHR in diverse extragonadal tissues is also closely related to Alzheimer's disease and cancers. Analysing the structural characteristics of the receptor is important in understanding the pathophysiology of diseases associated with the receptor. In this present study, homology modelling of FSHR-TM domain was developed using four different templates. Totally 20 models were developed using single template-based approach and selected three based on the validation of RC plot, RMSD, ProSA, QMEAN and ERRAT values. The developed models would be useful for further research on the structural characteristics and binding characteristics of the FSHR-TM domain.

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References

  1. Anderson RC, Newton CL, Millar RP. Small Molecule Follicle-Stimulating Hormone Receptor Agonists and Antagonists. Front Endocrinol (Lausanne) 2018;9:757.
  2. Yanofsky SD, Shen ES, Holden F, Whitehorn E, Aguilar B, Tate E, et al. Allosteric activation of the follicle-stimulating hormone (FSH) receptor by selective, nonpeptide agonists. J Biol Chem 2006;281(19):13226-33. https://doi.org/10.1074/jbc.M600601200
  3. Nataraja SG, Yu HN, Palmer SS. Discovery and Development of Small Molecule Allosteric Modulators of Glycoprotein Hormone Receptors. Front Endocrinol (Lausanne) 2015;6:142.
  4. Ulloa-Aguirre A, Zarinan T, Jardon-Valadez E, Gutierrez-Sagal R, Dias JA. Structure-Function Relationships of the Follicle-Stimulating Hormone Receptor. Front Endocrinol (Lausanne) 2018;9:707.
  5. Ulloa-Aguirre A, Reiter E, Crepieux P. FSH Receptor Signaling: Complexity of Interactions and Signal Diversity. Endocrinology 2018;159(8):3020-35. https://doi.org/10.1210/en.2018-00452
  6. Santhosh Kumar Nagarajan, Thirumurthy Madhavan. 3D Structure Prediction of Thromboxane A2 Receptor by Homology Modeling. J. Chosun Natural Sci.Vol. 8, No. 1 (2015) pp. 75 - 79. https://doi.org/10.13160/ricns.2015.8.1.75
  7. Altschul SF, Gish W, Miller W, Myers EW, Lipman DJ. Basic local alignment search tool. J Mol Biol 1990;215(3):403-10. https://doi.org/10.1016/S0022-2836(05)80360-2
  8. Kuntal BK, Aparoy P, Reddanna P. EasyModeller: A graphical interface to MODELLER. BMC Res Notes 2010;3:226.
  9. Pontius J, Richelle J, Wodak SJ. Deviationsfrom standard atomic volumes as a qualitymeasure for protein crystal structures. J Mol Biol 1996;264(1):121-36. https://doi.org/10.1006/jmbi.1996.0628
  10. Colovos C, Yeates TO. Verification of protein structures: patterns of nonbondedatomic interactions. Protein Sci 1993;2(9):1511-9. https://doi.org/10.1002/pro.5560020916
  11. Wiederstein M, Sippl MJ. ProSA-web: interactive web service for the recognitionof errors in three-dimensional structures of proteins. Nucleic Acids Res 2007;35(Web Server issue):W407-10. https://doi.org/10.1093/nar/gkm290
  12. Benkert P, Tosatto SCE, Schomburg D. QMEAN: A comprehensive scoring functionfor model quality assessment. Proteins 2008;71(1):261-77.