Molecular Playground/Hsp70-Hsp90: Difference between revisions
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==TPR Domain 1 Structure== | ==TPR Domain 1 Structure== | ||
TPR1 consists of 3 <scene name='56/566505/Tpr_motifs/2'>TPR motifs</scene> 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 <scene name='56/566505/Cbxy_clamp/2'>two-carboxylate clamp</scene> anchors the EEVD peptide motif of Hsp70 to TPR1 (residues highlighted in pink). | <scene name='56/566505/Tpr1/2'>TPR1</scene> consists of 3 <scene name='56/566505/Tpr_motifs/2'>TPR motifs</scene> 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 <scene name='56/566505/Cbxy_clamp/2'>two-carboxylate clamp</scene> anchors the EEVD peptide motif of Hsp70 to TPR1 (residues highlighted in pink). | ||