| Title: | COMPUTATIONAL MODELS OF THE SEVEN-HELIX TRANS-MEMBRANE HUMAN MELATONIN RECEPTOR MT1, ONE OF NATURE'S COMMON NANO-ASSEMBLIES |
| DOI No: | 10.1142/9789812701879_0048 |
| Source: | CLUSTERS AND NANO-ASSEMBLIES (pp 415-422)
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| Author(s): | CHARLES M. CASTEVENS
Departments of Physics and Chemistry, Virginia Commonwealth University, Richmond, VA 23284, USA
DONALD D. SHILLADY
Departments of Physics and Chemistry, Virginia Commonwealth University, Richmond, VA 23284, USA
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| Abstract: | In recent years it has been discovered that nature uses slight variations in a common nano-assembly of seven nearly parallel alpha-helix structures across cell membranes to transmit biological signals. Over seventy of these seven-helix structures are now known and within that group up to 70 percent of the amino acid sequence is conserved; only slight modifications of the amino acid sequence provides a wide variety of functions. This work models the human melatonin receptor MT1. Melatonin is a hormone produced by the pineal gland at night, and regulates sleep in humans and other animals. Theoretical research is being done to find a quick and inexpensive computational model of the trans-membrane (3300+ atoms) receptor and the ligands that bind to it as a way to guide experimental work. The SYBYL-HINT computer programs were used to study this nano-assembly of over 300 amino acids. Good agreement was found relating the computational binding energies and experimental equilibrium dissociation constants over six orders of magnitude for melatonin and twenty-four similar compounds. |
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