Structure and function of Escherichia coli DnaB protein: Role of the N-terminal domain in helicase activity

Biochemistry ◽  
1994 ◽  
Vol 33 (37) ◽  
pp. 11307-11314 ◽  
Author(s):  
Subhasis B. Biswas ◽  
Pei-Hua Chen ◽  
Esther E. Biswas
2013 ◽  
Vol 4 (1) ◽  
Author(s):  
Claire Bagnéris ◽  
Paul G. DeCaen ◽  
Benjamin A. Hall ◽  
Claire E. Naylor ◽  
David E. Clapham ◽  
...  

2011 ◽  
Vol 1807 (1) ◽  
pp. 36-41 ◽  
Author(s):  
Marina Verkhovskaya ◽  
Juho Knuuti ◽  
Mårten Wikström

2002 ◽  
Vol 42 (supplement2) ◽  
pp. S148
Author(s):  
T. Ohkubo ◽  
H. Takinowaki ◽  
Y. Matsuda ◽  
T. Yoshida ◽  
Y. Kobayashi

Author(s):  
Mubarak A. Alamri ◽  
Ahmed D. Alafnan ◽  
Obaid Afzal ◽  
Alhumaidi B. Alabbas ◽  
Safar M. Alqahtani

Background: The STE20/SPS1-related proline/alanine-rich kinase (SPAK) is a component of WNKSPAK/OSR1 signaling pathway that plays an essential role in blood pressure regulation. The function of SPAK is mediated by its highly conserved C-terminal domain (CTD) that interacts with RFXV/I motifs of upstream activators, WNK kinases, and downstream substrate, cation-chloride cotransporters. Objective: To determine and validate the three-dimensional structure of the CTD of SPAK and to study and analyze its interaction with the RFXV/I motifs. Methods: A homology model of SPAK CTD was generated and validated through multiple approaches. The model was based on utilizing the OSR1 protein kinase as a template. This model was subjected to 100 ns molecular dynamic (MD) simulation to evaluate its dynamic stability. The final equilibrated model was used to dock the RFQV-peptide derived from WNK4 into the primary pocket that was determined based on the homology sequence between human SPAK and OSR1 CTDs. The mechanism of interaction, conformational rearrangement and dynamic stability of the binding of RFQV-peptide to SPAK CTD were characterized by molecular docking and molecular dynamic simulation. Results: The MD simulation suggested that the binding of RFQV induces a large conformational change due to the distribution of salt bridge within the loop regions. These results may help in understanding the relation between the structure and function of SPAK CTD and to support drug design of potential SPAK kinase inhibitors as antihypertensive agents. Conclusion: This study provides deep insight into SPAK CTD structure and function relationship.


2020 ◽  
Vol 118 (3) ◽  
pp. 258a
Author(s):  
Laszlo Csernoch ◽  
Mónika Gönczi ◽  
Zsolt Ráduly ◽  
László Szabó ◽  
Nóra Dobrosi ◽  
...  

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