Báo cáo khoa học: A hydrophobic segment within the C-terminal domain is essential for both client-binding and dimer formation of the HSP90-family molecular chaperone
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Thea isoform of human 90-kDa heat shock protein(HSP90a) is composed of three domains: the N-terminal(residues 1–400); middle (residues 401–615) and C-terminal(residues 621–732). The middle domain is simultaneouslyassociated with the N- and C-terminal domains, and theinteractionwith the lattermediates thedimeric configurationof HSP90. Besides one in the N-terminal domain, an addi-tional client-binding site exists in the C-terminal domain ofHSP90.
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Báo cáo khoa học: A hydrophobic segment within the C-terminal domain is essential for both client-binding and dimer formation of the HSP90-family molecular chaperone
Nội dung trích xuất từ tài liệu:
Báo cáo khoa học: A hydrophobic segment within the C-terminal domain is essential for both client-binding and dimer formation of the HSP90-family molecular chaperone
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