scholarly journals Versatile allosteric properties in Pex5‐like tetratricopeptide repeat proteins to induce diverse downstream function

Traffic ◽  
2021 ◽  
Vol 22 (5) ◽  
pp. 140-152
Author(s):  
Jérôme Bürgi ◽  
Lakhan Ekal ◽  
Matthias Wilmanns
Keyword(s):  
Tetratricopeptide Repeat ◽  
Repeat Proteins ◽  
Tetratricopeptide Repeat Proteins ◽  
Allosteric Properties

Inhibition of eukaryotic translation by tetratricopeptide-repeat proteins of Orientia tsutsugamushi

2016 ◽  
Vol 54 (2) ◽  
pp. 136-144 ◽  
Author(s):  
Sunyoung Bang ◽  
Chan-Ki Min ◽  
Na-Young Ha ◽  
Myung-Sik Choi ◽  
Ik-Sang Kim ◽  
...  
Keyword(s):  
Tetratricopeptide Repeat ◽  
Orientia Tsutsugamushi ◽  
Eukaryotic Translation ◽  
Repeat Proteins ◽  
Tetratricopeptide Repeat Proteins

scholarly journals Molecular Dynamics Simulations of Consensus Tetratricopeptide Repeat Proteins

2010 ◽  
Vol 98 (3) ◽  
pp. 636a-637a
Author(s):  
Rudesh D. Toofanny ◽  
Aitziber L. Cortajarena ◽  
Lynne Regan ◽  
Valerie Daggett
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulations ◽  
Tetratricopeptide Repeat ◽  
Repeat Proteins ◽  
Tetratricopeptide Repeat Proteins ◽  
Dynamics Simulations

scholarly journals What Curves α-Solenoids?

2002 ◽  
Vol 277 (51) ◽  
pp. 49791-49798 ◽  
Author(s):  
Andrey V. Kajava
Keyword(s):  
Structural Model ◽  
Quaternary Structure ◽  
Tetratricopeptide Repeat ◽  
Protein Substrates ◽  
Unfolded Protein ◽  
Curved Structures ◽  
Repeat Proteins ◽  
Pattern Characteristic ◽  
The Common ◽  
Tetratricopeptide Repeat Proteins

The α-helical solenoid proteins adopt a variety of elongated curved structures. They have been examined to identify the interactions that determine their curvature. A sequence pattern characteristic for strongly curved α-helical solenoids has been constructed and was found to match protein sequences containing the proteasome/cyclosome repeats. Based on this, a structural model of the repeat-containing domains of the Rpn1/S2 and Rpn2/S1 proteins, which represent the largest subunits of the 26 S proteasome, has been proposed. The model has a novel architecture resembling an α-helical toroid. Molecular modeling shows that these toroids have a central pore that would allow passage of an unfolded protein substrate through it. This implies that the Rpn1 and Rpn2 toroids are aligned along the common axial pores of the ATPase hexamer and form an “antechamber” of the 26 S proteasome. The proposed quaternary structure agrees with the available experimental data. It is suggested that the function of this antechamber is assistance to the ATPases in the unfolding of protein substrates prior to proteolysis. An evolutionary link between the PC repeat-containing proteins and tetratricopeptide repeat proteins is proposed.

scholarly journals Interactions of S100A2 and S100A6 with the Tetratricopeptide Repeat Proteins, Hsp90/Hsp70-organizing Protein and Kinesin Light Chain

2008 ◽  
Vol 283 (42) ◽  
pp. 28246-28258 ◽  
Author(s):  
Seiko Shimamoto ◽  
Maki Takata ◽  
Masaaki Tokuda ◽  
Fumikazu Oohira ◽  
Hiroshi Tokumitsu ◽  
...  
Keyword(s):  
Light Chain ◽  
Tetratricopeptide Repeat ◽  
Kinesin Light Chain ◽  
Repeat Proteins ◽  
Tetratricopeptide Repeat Proteins
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