7XC0

Crystal structure of Human RPTPH

7XC0 の概要

• エントリーDOI: 10.2210/pdb7xc0/pdb
• 分子名称: Receptor-type tyrosine-protein phosphatase H, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: phosphatase, hydrolase
• 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: 33322.48

構造登録者

Kim, M.,Ryu, S.E. (登録日: 2022-03-22, 公開日: 2022-07-06, 最終更新日: 2023-11-29)

主引用文献

Kim, M.,Ryu, S.E.
Crystal structure of the catalytic domain of human RPTPH.
Acta Crystallogr.,Sect.F, 78:265-269, 2022

PubMed Abstract: Receptor-type protein tyrosine phosphatases (RPTPs) receive extracellular stimuli and transfer them into cells. They regulate cell growth, differentiation and death via specific signals. They have also been implicated in cancer, diabetes and neurological diseases. RPTPH, a member of the type 3 RPTP (R3-PTP) family, is an important regulator of colorectal cancer and hepatic carcinoma. Despite its importance in drug development, the structure of RPTPH has not yet been resolved. Here, the crystal structure of the catalytic domain of RPTPH was determined at 1.56 Å resolution. Despite similarities to other R3-PTPs in its overall structure, RPTPH exhibited differences in its loop regions and side-chain conformations. Compared with other R3-PTPs, RPTPH has unique side chains near its active site that may confer specificity for inhibitor binding. Therefore, detailed information on the structure of RPTPH provides clues for the development of specific inhibitors.

PubMed: 35787553
DOI: 10.1107/S2053230X22006173

実験手法

X-RAY DIFFRACTION (1.56 Å)