1CB0

STRUCTURE OF HUMAN 5'-DEOXY-5'-METHYLTHIOADENOSINE PHOSPHORYLASE AT 1.7 A RESOLUTION

1CB0 の概要

• エントリーDOI: 10.2210/pdb1cb0/pdb
• 分子名称: PROTEIN (5'-DEOXY-5'-METHYLTHIOADENOSINE PHOSPHORYLASE), ADENINE (3 entities in total)
• 機能のキーワード: methylthioadenosine phosphorylase, purine nucleoside phosphorylase, purine salvage, adenine, transferase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31412.18

構造登録者

Appleby, T.C.,Erion, M.D.,Ealick, S.E. (登録日: 1999-02-26, 公開日: 1999-07-05, 最終更新日: 2023-12-27)

主引用文献

Appleby, T.C.,Erion, M.D.,Ealick, S.E.
The structure of human 5'-deoxy-5'-methylthioadenosine phosphorylase at 1.7 A resolution provides insights into substrate binding and catalysis.
Structure Fold.Des., 7:629-641, 1999

PubMed Abstract: 5'-Deoxy-5'-methylthioadenosine phosphorylase (MTAP) catalyzes the reversible phosphorolysis of 5'-deoxy-5'-methylthioadenosine (MTA) to adenine and 5-methylthio-D-ribose-1-phosphate. MTA is a by-product of polyamine biosynthesis, which is essential for cell growth and proliferation. This salvage reaction is the principle source of free adenine in human cells. Because of its importance in coupling the purine salvage pathway to polyamine biosynthesis MTAP is a potential chemotherapeutic target.

PubMed: 10404592
DOI: 10.1016/S0969-2126(99)80084-7

実験手法

X-RAY DIFFRACTION (1.7 Å)