1JQE

Crystal Structure Analysis of Human Histamine Methyltransferase (Ile105 Polymorphic Variant) Complexed with AdoHcy and Antimalarial Drug Quinacrine

Summary for 1JQE

• Entry DOI: 10.2210/pdb1jqe/pdb
• Related: 1JQD
• Descriptor: Histamine N-Methyltransferase, S-ADENOSYL-L-HOMOCYSTEINE, QUINACRINE, ... (5 entities in total)
• Functional Keywords: classic methyltransferase fold, protein-substrate-cofactor complex, polymorphic variant, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm : P50135
• Total number of polymer chains: 2
• Total formula weight: 67858.92

Authors

Horton, J.R.,Sawada, K.,Nishibori, M.,Zhang, X.,Cheng, X. (deposition date: 2001-08-06, release date: 2002-08-06, Last modification date: 2024-04-03)

Primary citation

Horton, J.R.,Sawada, K.,Nishibori, M.,Zhang, X.,Cheng, X.
Two polymorphic forms of human histamine methyltransferase: structural, thermal, and kinetic comparisons.
Structure, 9:837-849, 2001

PubMed Abstract: Histamine plays important biological roles in cell-to-cell communication; it is a mediator in allergic responses, a regulator of gastric acid secretion, a messenger in bronchial asthma, and a neurotransmitter in the central nervous system. Histamine acts by binding to histamine receptors, and its local action is terminated primarily by methylation. Human histamine N-methyltransferase (HNMT) has a common polymorphism at residue 105 that correlates with the high- (Thr) and low- (Ile) activity phenotypes.

PubMed: 11566133
DOI: 10.1016/S0969-2126(01)00643-8

Experimental method

X-RAY DIFFRACTION (1.91 Å)