Interdomain Linker Determines Primarily the Structural Stability of Dystrophin and Utrophin Tandem Calponin-Homology Domains Rather than Their Actin-Binding Affinity

Biochemistry ◽  
2015 ◽  
Vol 54 (35) ◽  
pp. 5480-5488 ◽  
Author(s):  
Swati Bandi ◽  
Surinder M. Singh ◽  
Krishna M. G. Mallela
Keyword(s):  
Binding Affinity ◽  
Structural Stability ◽  
Actin Binding ◽  
Calponin Homology ◽  
Interdomain Linker ◽  
Homology Domains

Novel structural insights into F-actin-binding and novel functions of calponin homology domains

2008 ◽  
Vol 18 (6) ◽  
pp. 702-708 ◽  
Author(s):  
Björn Sjöblom ◽  
Jari Ylänne ◽  
Kristina Djinović-Carugo
Keyword(s):  
Actin Binding ◽  
Calponin Homology ◽  
Structural Insights ◽  
Homology Domains

scholarly journals Single calponin homology domains are not actin-binding domains

1998 ◽  
Vol 8 (19) ◽  
pp. R673-R675 ◽  
Author(s):  
Mario Gimona ◽  
Steven J. Winder
Keyword(s):  
Actin Binding ◽  
Calponin Homology ◽  
Binding Domains ◽  
Homology Domains

The Actin Binding Affinity of the Utrophin Tandem Calponin-Homology Domain Is Primarily Determined by Its N-Terminal Domain

Biochemistry ◽  
2014 ◽  
Vol 53 (11) ◽  
pp. 1801-1809 ◽  
Author(s):  
Surinder M. Singh ◽  
Swati Bandi ◽  
Steve J. Winder ◽  
Krishna M. G. Mallela
Keyword(s):  
Binding Affinity ◽  
Actin Binding ◽  
Calponin Homology Domain ◽  
Calponin Homology ◽  
Terminal Domain

scholarly journals Tug-Of-War Between Thermodynamic Stability and Actin-Binding Function of Tandem Calponin-Homology Domains

2014 ◽  
Vol 106 (2) ◽  
pp. 467a-468a
Author(s):  
Swati Bandi ◽  
Surinder Singh ◽  
Geoffrey Armstrong ◽  
Krishna Mallela
Keyword(s):  
Thermodynamic Stability ◽  
Actin Binding ◽  
Calponin Homology ◽  
Binding Function ◽  
Homology Domains

scholarly journals Steric regulation of tandem calponin homology domain actin-binding affinity

2019 ◽  
Vol 30 (26) ◽  
pp. 3112-3122 ◽  
Author(s):  
Andrew R. Harris ◽  
Brian Belardi ◽  
Pamela Jreij ◽  
Kathy Wei ◽  
Hengameh Shams ◽  
...  
Keyword(s):  
Subcellular Localization ◽  
Binding Affinity ◽  
Actin Binding ◽  
Calponin Homology Domain ◽  
Calponin Homology ◽  
Flanking Region

We show that the affinity of CH1–CH2 domains for F-actin can be both increased and decreased by diverse modifications that change the effective “openness” of CH1 and CH2, which sterically regulates binding to F-actin. We also show that subcellular localization depends on the N-terminal flanking region of CH1 but not on the overall affinity for F-actin.

scholarly journals Structural comparisons of calponin homology domains: implications for actin binding

Structure ◽  
1998 ◽  
Vol 6 (11) ◽  
pp. 1419-1431 ◽  
Author(s):  
Sonia Bañuelos ◽  
Matti Saraste ◽  
Kristina Djinović Carugo
Keyword(s):  
Actin Binding ◽  
Calponin Homology ◽  
Homology Domains

scholarly journals Large-scale opening of utrophin's tandem calponin homology (CH) domains upon actin binding by an induced-fit mechanism

2011 ◽  
Vol 108 (31) ◽  
pp. 12729-12733 ◽  
Author(s):  
A. Y. Lin ◽  
E. Prochniewicz ◽  
Z. M. James ◽  
B. Svensson ◽  
D. D. Thomas
Keyword(s):  
Large Scale ◽  
Actin Binding ◽  
Induced Fit ◽  
Calponin Homology
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