H-1, N-15 and C-13 resonance assignments of the Tetratricopeptide Repeat (TPR) domain of hSGT

[[abstract]]TPR-containing proteins are involved in a diverse spectrum of cellular functions including cell cycle control, splicing and transcription, protein transport, regulating protein phosphorylation, and protein folding (Blatch and Lassle, 1999; Lamb et al., 1995). TPR motifs often exist as an array with 3 to 25 repeated units to form a characteristic structure in different proteins, and there is no preferential positioning of the motifs along the primary structure of the proteins. Each TPR motif contains 34 residues and forms two α-helices of equal length, known as A- and B-helix, associated with a packing angle of approximately 24◦ between the helix axes (Das et al., 1998). Adjacent TPR motifs are packed together in a parallel arrangement, such that sequentially adjacent α-helices are antiparallel. The consequence of this uniform angular and spatial arrangement of neighboring α helices creates a right-handed superhelical structure featuring an amphipathic channel that might accommodate the complementary region of a target protein (Das et al., 1998).[[fileno]]2050103010012[[department]]生科