The TPR Motif as a Protein Interaction Module – A Discussion of Structure and Function
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چکیده
منابع مشابه
The crystal structure of NlpI. A prokaryotic tetratricopeptide repeat protein with a globular fold.
There are several different families of repeat proteins. In each, a distinct structural motif is repeated in tandem to generate an elongated structure. The nonglobular, extended structures that result are particularly well suited to present a large surface area and to function as interaction domains. Many repeat proteins have been demonstrated experimentally to fold and function as independent ...
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The tetratricopeptide repeat (TPR) motif is a protein-protein interaction module that acts as an organizing centre for complexes regulating a multitude of biological processes. Despite accumulating evidence for the formation of TPR oligomers as an additional level of regulation there is a lack of structural and solution data explaining TPR self-association. In the present work we characterize t...
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Tetratricopeptide (TPR) domains are known protein interaction domains. We show that the TPR domain of FKBP8 selectively binds Hsp90, and interactions upstream of the conserved MEEVD motif are critical for tight binding. In contrast FKBP8 failed to bind intact Hsp70. The PPIase domain was not essential for the interaction with Hsp90 and binding was completely encompassed by the TPR domain alone....
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a key factor in spermatogenesis and disorders associated with this protein have been recognized to be related to male infertility. Although it was suggested that this protein could have different functions during germ cell development, no studies have been conducted to uncover the mechanism of this potential function yet. Here, we analyzed the expression pattern of RBMY protein isoforms in test...
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a parallel array, to produce an extended molecule with an overall superhelical architecture. This can be visualized as a spiral staircase in which the individual TPR and Biochemistry motifs are the steps. Precisely how the TPR fold may mediate protein-pro-2 Howard Hughes Medical Institute 3 Department of Chemistry tein interactions was first revealed by the crystal structures of the two differe...
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