P.1.e.009 The neural correlates of reduced dopamine and serotonin in mood and reinforcement

Abstract

The modified purine nucleotide 8-oxo-guanosine-2′-phosphate binds at the pyrimidine binding site of ribonuclease-A. The O8-2′GMP inhibitor is in a syn conformation, with an intramolecular hydrogen bond between the N-3 atom of the base and the O-5′ atom of the ribose. The essential groups of the protein involved in base recognition are Oγ45 and N-45, which form hydrogen bonds to the five-membered ring of the heterocyclic base. Mobility of enzyme side-chains (viz. LyThe modified purine nucleotide 8-oxo-guanosine-2′-phosphate binds at the pyrimidine binding site of ribonuclease-A. The O8-2′GMP inhibitor is in a syn conformation, with an intramolecular hydrogen bond between the N-3 atom of the base and the O-5′ atom of the ribose. The essential groups of the protein involved in base recognition are Oγ45 and N-45, which form hydrogen bonds to the five-membered ring of the heterocyclic base. Mobility of enzyme side-chains (viz. LyThe modified purine nucleotide 8-oxo-guanosine-2′-phosphate binds at the pyrimidine binding site of ribonuclease-A. The O8-2′GMP inhibitor is in a syn conformation, with an intramolecular hydrogen bond between the N-3 atom of the base and the O-5′ atom of the ribose. The essential groups of the protein involved in base recognition are Oγ45 and N-45, which form hydrogen bonds to the five-membered ring of the heterocyclic base. Mobility of enzyme side-chains (viz. LyThe modified purine nucleotide 8-oxo-guanosine-2′-phosphate binds at the pyrimidine binding site of ribonuclease-A. The O8-2′GMP inhibitor is in a syn conformation, with an intramolecular hydrogen bond between the N-3 atom of the base and the O-5′ atom of the ribose. The essential groups of the protein involved in base recognition are Oγ45 and N-45, which form hydrogen bonds to the five-membered ring of the heterocyclic base. Mobility of enzyme side-chains (viz. Lys41, Lys66, Hisl119) close to the catalytic cleft of the protein allows conformational flexibility in the substrate binding region of ribonuclease-A. Inhibitor binding alters the solvent structure of the protein but the overall shape of the enzyme is not effected.1, Lys66, Hisl119) close to the catalytic cleft of the protein allows conformational flexibility in the substrate binding region of ribonuclease-A. Inhibitor binding alters the solvent structure of the protein but the overall shape of the enzyme is not effected.1, Lys66, Hisl119) close to the catalytic cleft of the protein allows conformational flexibility in the substrate binding region of ribonuclease-A. Inhibitor binding alters the solvent structure of the protein but the overall shape of the enzyme is not effected.1, Lys66, Hisl119) close to the catalytic cleft of the protein allows conformational flexibility in the substrate binding region of ribonuclease-A. Inhibitor binding alters the solvent structure of the protein but the overall shape of the enzyme is not effected.