Cooperative Ordering in Homeodomain−DNA Recognition:  Solution Structure and Dynamics of the MATa1 Homeodomain†

Biochemistry ◽  
2000 ◽  
Vol 39 (33) ◽  
pp. 10045-10054 ◽  
Author(s):  
Janet S. Anderson ◽  
Michael D. Forman ◽  
Sarah Modleski ◽  
Frederick W. Dahlquist ◽  
Susan M. Baxter
Keyword(s):  
Solution Structure ◽  
Dna Recognition ◽  
Structure And Dynamics ◽  
Cooperative Ordering

Solution structure and dynamics of glia maturation factor from Caenorhabditis elegans

2018 ◽  
Vol 1866 (10) ◽  
pp. 1008-1020 ◽  
Author(s):  
Diva Maheshwari ◽  
Vaibhav Kumar Shukla ◽  
Anupam Jain ◽  
Sarita Tripathi ◽  
Dinesh Kumar ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Solution Structure ◽  
Glia Maturation Factor ◽  
Structure And Dynamics ◽  
Maturation Factor

scholarly journals Unraveling the structure and dynamics of the human DNAJB6b chaperone by NMR reveals insights into Hsp40-mediated proteostasis

2019 ◽  
Vol 116 (43) ◽  
pp. 21529-21538 ◽  
Author(s):  
Theodoros K. Karamanos ◽  
Vitali Tugarinov ◽  
G. Marius Clore
Keyword(s):  
Solution Structure ◽  
Specific Substrate ◽  
Monomeric Form ◽  
Linker Region ◽  
Structure And Dynamics ◽  
J Domain ◽  
Folded Proteins ◽  
High Flexibility ◽  
Interdomain Interactions ◽  
Shed Light

J-domain chaperones are involved in the efficient handover of misfolded/partially folded proteins to Hsp70 but also function independently to protect against cell death. Due to their high flexibility, the mechanism by which they regulate the Hsp70 cycle and how specific substrate recognition is performed remains unknown. Here we focus on DNAJB6b, which has been implicated in various human diseases and represents a key player in protection against neurodegeneration and protein aggregation. Using a variant that exists mainly in a monomeric form, we report the solution structure of an Hsp40 containing not only the J and C-terminal substrate binding (CTD) domains but also the functionally important linkers. The structure reveals a highly dynamic protein in which part of the linker region masks the Hsp70 binding site. Transient interdomain interactions via regions crucial for Hsp70 binding create a closed, autoinhibited state and help retain the monomeric form of the protein. Detailed NMR analysis shows that the CTD (but not the J domain) self-associates to form an oligomer comprising ∼35 monomeric units, revealing an intricate balance between intramolecular and intermolecular interactions. The results shed light on the mechanism of autoregulation of the Hsp70 cycle via conserved parts of the linker region and reveal the mechanism of DNAJB6b oligomerization and potentially antiaggregation.

Solution Structure and Dynamics of Cartilage Aggrecan

2006 ◽  
Vol 7 (7) ◽  
pp. 2162-2172 ◽  
Author(s):  
A. Papagiannopoulos ◽  
T. A. Waigh ◽  
T. Hardingham ◽  
M. Heinrich
Keyword(s):  
Solution Structure ◽  
Structure And Dynamics

Solution structure and dynamics of S100A5 in the apo and Ca2+-bound states

2009 ◽  
Vol 14 (7) ◽  
pp. 1097-1107 ◽  
Author(s):  
Ivano Bertini ◽  
Soumyasri Das Gupta ◽  
Xiaoyu Hu ◽  
Tilemachos Karavelas ◽  
Claudio Luchinat ◽  
...  
Keyword(s):  
Bound States ◽  
Solution Structure ◽  
Structure And Dynamics

Solution structure and dynamics of human S100A14

2012 ◽  
Vol 18 (2) ◽  
pp. 183-194 ◽  
Author(s):  
Ivano Bertini ◽  
Valentina Borsi ◽  
Linda Cerofolini ◽  
Soumyasri Das Gupta ◽  
Marco Fragai ◽  
...  
Keyword(s):  
Solution Structure ◽  
Structure And Dynamics
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