PDBsum entry: 1rpm

Receptor

PDB id: 1rpm

Contents

Protein chains

278 a.a. *

Waters ×350

* Residue conservation analysis

PDB id:

1rpm

Name:

Receptor

Title:

Human receptor protein tyrosine phosphatase mu, domain 1

Structure:

Receptor protein tyrosine phosphatase mu. Chain: a, b. Fragment: cytosolic membrane proximal catalytic domain. Synonym: d1. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.30Å R-factor: 0.195 R-free: 0.260

Authors:

K.M.V.Hoffmann,N.K.Tonks,D.Barford

Key ref:

K.M.Hoffmann et al. (1997). The crystal structure of domain 1 of receptor protein-tyrosine phosphatase mu. J Biol Chem, 272, 27505-27508. PubMed id: 9346878 DOI: 10.1074/jbc.272.44.27505

Date:

11-Sep-97 Release date: 01-Apr-98

Protein chains

P28827  (PTPRM_HUMAN) -  Receptor-type tyrosine-protein phosphatase mu

Seq: 1452 a.a.

Struc: 278 a.a.

Enzyme reactions

• Enzyme class: E.C.3.1.3.48 - Protein-tyrosine-phosphatase.
• Reaction: Protein tyrosine phosphate + H₂O = protein tyrosine + phosphate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Biological process: dephosphorylation (2 terms)
• Biochemical function: phosphatase activity (2 terms)

reference

DOI no: 10.1074/jbc.272.44.27505

J Biol Chem 272:27505-27508 (1997)

PubMed id: 9346878

The crystal structure of domain 1 of receptor protein-tyrosine phosphatase mu.

K.M.Hoffmann, N.K.Tonks, D.Barford.

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.

Selected figure(s)

Figure 1.
Fig. 1. Ribbon diagram of the receptor PTPµ D1 dimer. The molecular dyad axis is indicated by an arrow. The catalytic site^ cysteine (Cys1095), the helix-turn-helix segment ( 1 , 2 ), and the N-terminal -strand ( x) that forms a -sheet with y within RPTPs D1 are^ indicated within one subunit (left). The 8 and 10 strands participate^ in the dimer interface of RPTPµ D1. C atoms of the equivalent catalytic site residues that form the dimer interface of RPTP D1 are shown as spheres and labeled. Figure was drawn using MOLSCRIPT (22).

Figure 3.
Fig. 3. Sequence alignment of representative RPTP D1s in the regions that form the dimer interfaces of RPTP and RPTPµ. Top left, x-helix-turn-helix segment; top right, residues of the^ Tyr(P) recognition loop of the catalytic site. Bottom, residues from 8 through to the WPD loop of the catalytic site. Residues of RPTPµ D1 and RPTP D1 that form interactions at their respective^ dimer interfaces are indicated with vertical arrows (top) and^ stars (bottom), respectively. The residues that form the dimer interface of RPTPµ D1 are poorly conserved throughout the family, whereas residues of the RPTP D1 interface are poorly conserved^ within the helix-turn-helix segment, but well conserved within the catalytic site. Invariant residues are in white type on a^ black background, and highly conserved residues are boxed.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (1997, 272, 27505-27508) copyright 1997.

Figures were selected by an automated process.