A Three-Dimensional Model for the Interaction of MSH with the Melanocortin-1 Receptor

A model for the interaction of the melanocortin-1 (MC1) receptor with MSH peptide has been constructed. The model was built by homology modelling using bacteriorhodopsin as template. A cyclic analogue of MSH could be docked into a binding pocket located between transmembrane (TM) domains 2, 3 and 6...

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Veröffentlicht in:	Biochemical and biophysical research communications 1995-05, Vol.210 (1), p.205-210
Hauptverfasser:	Prusis, P., Frandberg, P.A., Muceniece, R., Kalvinsh, I., Wikberg, J.E.S.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Computer Simulation Ligands Melanocyte-Stimulating Hormones - chemistry Melanocyte-Stimulating Hormones - metabolism Models, Molecular Molecular Sequence Data Peptides, Cyclic - chemistry Protein Structure, Tertiary Receptors, Pituitary Hormone - metabolism Receptors, Pituitary Hormone - ultrastructure Sequence Alignment Sequence Homology, Amino Acid
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Beschreibung
Zusammenfassung:	A model for the interaction of the melanocortin-1 (MC1) receptor with MSH peptide has been constructed. The model was built by homology modelling using bacteriorhodopsin as template. A cyclic analogue of MSH could be docked into a binding pocket located between transmembrane (TM) domains 2, 3 and 6 of the receptor. The most significant receptor to ligand interactions occur between D117 in TM3 of receptor with histidine in cyclic MSH-peptide, H260 in TM6 with glutamic in peptide and D121 in TM3 with arginine in peptide. The model finds support from earlier mutagenesis data.
ISSN:	0006-291X 1090-2104
DOI:	10.1006/bbrc.1995.1647