1rpm
From Proteopedia
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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
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