This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1rpm
From Proteopedia
|
HUMAN RECEPTOR PROTEIN TYROSINE PHOSPHATASE MU, DOMAIN 1
Overview
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 ... [(full description)]
About this Structure
1RPM is a [Single protein] structure of sequence from [Homo sapiens]. Active as [[1]], with EC number [3.1.3.48]. Full crystallographic information is available from [OCA].
Reference
The crystal structure of domain 1 of receptor protein-tyrosine phosphatase mu., Hoffmann KM, Tonks NK, Barford D, J Biol Chem. 1997 Oct 31;272(44):27505-8. PMID:9346878
Page seeded by OCA on Mon Oct 29 22:05:53 2007
