1LAR

CRYSTAL STRUCTURE OF THE TANDEM PHOSPHATASE DOMAINS OF RPTP LAR

1LAR の概要

• エントリーDOI: 10.2210/pdb1lar/pdb
• 分子名称: PROTEIN (LAR) (2 entities in total)
• 機能のキーワード: tyrosine phosphatease, lar protein, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P10586
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 132184.19

構造登録者

Nam, H.-J.,Poy, F.,Krueger, N.,Saito, H.,Frederick, C.A. (登録日: 1999-04-20, 公開日: 2000-04-25, 最終更新日: 2023-08-16)

主引用文献

Nam, H.J.,Poy, F.,Krueger, N.X.,Saito, H.,Frederick, C.A.
Crystal structure of the tandem phosphatase domains of RPTP LAR.
Cell(Cambridge,Mass.), 97:449-457, 1999

PubMed Abstract: Most receptor-like protein tyrosine phosphatases (RPTPs) contain two conserved phosphatase domains (D1 and D2) in their intracellular region. The carboxy-terminal D2 domain has little or no catalytic activity. The crystal structure of the tandem D1 and D2 domains of the human RPTP LAR revealed that the tertiary structures of the LAR D1 and D2 domains are very similar to each other, with the exception of conformational differences at two amino acid positions in the D2 domain. Site-directed mutational changes at these positions (Leu-1644-to-Tyr and Glu-1779-to-Asp) conferred a robust PTPase activity to the D2 domain. The catalytic sites of both domains are accessible, in contrast to the dimeric blocked orientation model previously suggested. The relative orientation of the LAR D1 and D2 domains, constrained by a short linker, is stabilized by extensive interdomain interactions, suggesting that this orientation might be favored in solution.

PubMed: 10338209
DOI: 10.1016/S0092-8674(00)80755-2

実験手法

X-RAY DIFFRACTION (2 Å)