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Medicinal Chemistry Research

, Volume 20, Issue 9, pp 1704–1712 | Cite as

Homology modeling of human CCR2 receptor

  • Rajesh Singh
  • M. Elizabeth Sobhia
Original Research

Abstract

Homology model of CCR2 receptor was built on the basis of the crystal structure of human beta-2 adrenoceptor (PDB ID-2RH1). The model showed 99.3% residues in the core and allowed regions of the Ramachandran plot and there was no residue present in the disallowed regions. Prosa2003 program was used to assess the model and it displayed good native protein folding. The model also provided good root mean square deviation (RMSD) value and alignment score with the template, human β2-adrenoceptor. The binding site is found within the transmembrane (TM) region and is sufficiently large enough for docking the known CCR2 ligands. The docking results validated the homology model to meet various criteria that are necessary in molecular modeling studies.

Keywords

Homology modeling Docking Chemokine receptor CCR2 MCP-1 CC-chemokine receptor 2 Monocyte chemoattractant protein-1 

Notes

Acknowledgments

The authors thank the Council of Scientific and Industrial Research (CSIR) and the Department of Science and Technology (DST) for financial support.

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Copyright information

© Springer Science+Business Media, LLC 2010

Authors and Affiliations

  1. 1.Department of PharmacoinformaticsNational Institute of Pharmaceutical Education and Research (NIPER)MohaliIndia

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