TPR1</scene> consists of 3 TPR motifs and is responsible for the interaction with the C terminus of Hsp70. Mutation studies showed that the binding of TPR1 to Hsp70 is dependent upon the interaction between the TPR1 domain and a 12-mer C-terminal peptide of Hsp70 (GSGSGPTIEEVD). Shown to the right is the crystallized TPR1 with its respective Hsp70 peptide partner. TPR1 forms a cradle-like structure that accommodates the Hsp70 peptide in an extended conformation, and the peptide makes contact with only the sidechains of the helices in TPR1 that face the inner surface of the cradle. Additionally, a highly conserved two-carboxylate clamp anchors the EEVD peptide motif of Hsp70 to TPR1.
is an Endoplasmic Reticulum (ER) resident protein disulfide isomerase. It is a 793 amino acid multi-domain protein. It consists of an N-terminal that has been shown to bind to BIP, ER resident HSP70, four redox-active domains (displayed here in green) and their respective redox-active CXXC motifs labeled in red and two domains shown in yellow, which lack CXXC redox-active motifs.
References
1. D'Andrea, L. Regan, L. TiBS Review; 28:12. 2003
2. Scheufler, C. et. al. Cell; 101:199-210. 2000
3. Zeytuni, N. et. al. Cell Structure; 20. 2012
