Intra- and intermolecular interactions of the catalytic domains of human CD45 protein tyrosine phosphatase.
We have investigated protein-protein interaction between distinct domains of the human CD45 cytoplasmic region using a yeast two-hybrid system. Consequently, we have found that the spacer region between two tandem PTP domains specifically interacts with the membrane-distal PTP domain (D2). This interaction is mediated by a stretch of amino acid residues in the carboxyl-terminal half of the spacer region. Although the membrane proximal region does not directly interact with either of the two PTP domains, it appears to function in stabilizing the interaction between the spacer region and D2. We also demonstrate that the interaction between the spacer region and D2 might take place intramolecularly.
Hayami-Noumi
K
K
Department of Microbiology, Faculty of Pharmaceutical Sciences, Okayama University, 3-1-1 Tsushima-naka, Okayama, Japan.
Tsuchiya
T
T
Moriyama
Y
Y
Noumi
T
T
D020134:Catalytic Domain / Q000502:physiology*; D002462:Cell Membrane / Q000378:metabolism; D004795:Enzyme Stability / Q000235:genetics; D017493:Leukocyte Common Antigens / Q000235:genetics* / Q000378:metabolism*; D016297:Mutagenesis, Site-Directed; D010446:Peptide Fragments / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding / Q000235:genetics; D017510:Protein Folding; D017434:Protein Structure, Tertiary / Q000235:genetics; D020798:Two-Hybrid System Techniques; D015003:Yeasts
D010446:Peptide Fragments; D017493:Leukocyte Common Antigens