1RPM

HUMAN RECEPTOR PROTEIN TYROSINE PHOSPHATASE MU, DOMAIN 1

1RPM の概要

• エントリーDOI: 10.2210/pdb1rpm/pdb
• 分子名称: RECEPTOR PROTEIN TYROSINE PHOSPHATASE MU (2 entities in total)
• 機能のキーワード: receptor, phosphatase, signal transduction, adhesion, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P28827
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 64302.99

構造登録者

Hoffmann, K.M.V.,Tonks, N.K.,Barford, D. (登録日: 1997-09-11, 公開日: 1998-04-01, 最終更新日: 2024-05-22)

主引用文献

Hoffmann, K.M.,Tonks, N.K.,Barford, D.
The crystal structure of domain 1 of receptor protein-tyrosine phosphatase mu.
J.Biol.Chem., 272:27505-27508, 1997

PubMed Abstract: Receptor-like protein-tyrosine phosphatases (RPTPs) play important roles in regulating intracellular processes. We have been investigating the regulation and function of RPTPmu, a receptor-like PTP related to the Ig superfamily of cell adhesion molecules. Recently, the crystal structure of a dimer of the membrane proximal domain of RPTPalpha (RPTPalpha D1) was described (Bilwes, A. M., den Hertog, J., Hunter, T., and Noel J. P. (1996) Nature 382, 555-559). Within this crystal structure, the catalytic site of each subunit of the dimer is sterically blocked by the insertion of the N-terminal helix-turn-helix segment of the dyad-related monomer. It was proposed that dimerization would lead to inhibition of catalytic activity and may provide a paradigm for the regulation of the RPTP family. We have determined the crystal structure, to 2.3 A resolution, of RPTPmu D1, which shares 46% sequence identity with that of RPTPalpha D1. Although the tertiary structures of RPTPalpha D1 and RPTPmu D1 are very similar, with a root mean square deviation between equivalent Calpha atoms of 1.1 A, the quaternary structures of these two proteins are different. Neither the catalytic site nor the N-terminal helix-turn-helix segment of RPTPmu D1 participates in protein-protein interactions. The catalytic site of RPTPmu D1 is unhindered and adopts an open conformation similar to that of the cytosolic PTP, PTP1B (Barford, D., Flint, A. J., and Tonks, N. K. (1994) Science 263, 1397-1404). We propose that dimerization-induced modulation of RPTP activity may not be a general feature of this family of enzymes.

PubMed: 9346878
DOI: 10.1074/jbc.272.44.27505

実験手法

X-RAY DIFFRACTION (2.3 Å)