1HNN

CRYSTAL STRUCTURE OF HUMAN PNMT COMPLEXED WITH SK&F 29661 AND ADOHCY(SAH)

Summary for 1HNN

• Entry DOI: 10.2210/pdb1hnn/pdb
• Descriptor: PHENYLETHANOLAMINE N-METHYLTRANSFERASE, S-ADENOSYL-L-HOMOCYSTEINE, 1,2,3,4-TETRAHYDRO-ISOQUINOLINE-7-SULFONIC ACID AMIDE, ... (4 entities in total)
• Functional Keywords: methyltransferase, adrenaline synthesis, s-adenosyl methionine, transferase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 62969.32

Authors

Martin, J.L.,Begun, J.,McLeish, M.J.,Caine, J.M.,Grunewald, G.L. (deposition date: 2000-12-07, release date: 2001-12-07, Last modification date: 2024-02-07)

Primary citation

Martin, J.L.,Begun, J.,McLeish, M.J.,Caine, J.M.,Grunewald, G.L.
Getting the adrenaline going: crystal structure of the adrenaline-synthesizing enzyme PNMT.
Structure, 9:977-985, 2001

PubMed Abstract: Adrenaline is localized to specific regions of the central nervous system (CNS), but its role therein is unclear because of a lack of suitable pharmacologic agents. Ideally, a chemical is required that crosses the blood-brain barrier, potently inhibits the adrenaline-synthesizing enzyme PNMT, and does not affect other catecholamine processes. Currently available PNMT inhibitors do not meet these criteria. We aim to produce potent, selective, and CNS-active PNMT inhibitors by structure-based design methods. The first step is the structure determination of PNMT.

PubMed: 11591352
DOI: 10.1016/S0969-2126(01)00662-1

Experimental method

X-RAY DIFFRACTION (2.4 Å)