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TPR domain

TPR) domains. PP2B (calcineurin) is a heterodimer of a catalytic A-subunit together with a regulatory, Ca2+-binding B-subunit. The A-subunit additionally carries a calmodulin binding site and an autoinhibitory domain. PP7 also contains EF-hand motifs. Both, PP2B and PP7 are stimulated by Ca2+-ions. [Pg.1013]

P3H and CRTAP also have multiple TPR domains, which may be important in mediating... [Pg.493]

Fig. 10. Structural basis for TPR-domain binding. Structure of the middle TPR domain of Hop bound to a peptide corresponding to the C terminus of Hsp90 (Scheufler et al., 2000). The peptide binds in the groove formed by the superhelical arrangement of a-helices in the TPR domain, making specific interactions involving the side chains of the MEEVD sequence and the a-carboxyl of the terminal aspartic acid. Fig. 10. Structural basis for TPR-domain binding. Structure of the middle TPR domain of Hop bound to a peptide corresponding to the C terminus of Hsp90 (Scheufler et al., 2000). The peptide binds in the groove formed by the superhelical arrangement of a-helices in the TPR domain, making specific interactions involving the side chains of the MEEVD sequence and the a-carboxyl of the terminal aspartic acid.
Scheufler, C., Brinker, A., Bourenkov, G., Pegoraro, S., Moroder, L., Bartunik, H., Hard, F. U., and Moarefi, I. (2000). Structure of TPR domain-peptide complexes critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 101, 199-210. [Pg.120]


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See also in sourсe #XX -- [ Pg.265 , Pg.273 ]




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