1JQD

Crystal Structure Analysis of Human Histamine Methyltransferase (Thr105 Polymorphic Variant) Complexed with AdoHcy and Histamine

1JQD の概要

• エントリーDOI: 10.2210/pdb1jqd/pdb
• 関連するPDBエントリー: 1JQE
• 分子名称: Histamine N-Methyltransferase, S-ADENOSYL-L-HOMOCYSTEINE, HISTAMINE, ... (4 entities in total)
• 機能のキーワード: classic methyltransferase fold, protein-substrate-cofactor complex, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm : P50135
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 67657.15

構造登録者

Horton, J.R.,Sawada, K.,Nishibori, M.,Zhang, X.,Cheng, X. (登録日: 2001-08-06, 公開日: 2002-08-06, 最終更新日: 2024-04-03)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.28 Å)