scholarly journals Efficient Local Unfolding with Ancestor Stacks for Full Prolog

2005 ◽  
pp. 149-165 ◽  
Author(s):  
Germán Puebla ◽  
Elvira Albert ◽  
Manuel Hermenegildo
Keyword(s):  
Local Unfolding

scholarly journals Human Defensins Facilitate Local Unfolding of Thermodynamically Unstable Regions of Bacterial Protein Toxins

Immunity ◽  
2014 ◽  
Vol 41 (5) ◽  
pp. 709-721 ◽  
Author(s):  
Elena Kudryashova ◽  
Royston Quintyn ◽  
Stephanie Seveau ◽  
Wuyuan Lu ◽  
Vicki H. Wysocki ◽  
...  
Keyword(s):  
Bacterial Protein ◽  
Protein Toxins ◽  
Local Unfolding ◽  
Human Defensins

scholarly journals Structural Plasticity and Distinct Drug-Binding Modes of LfrR, a Mycobacterial Efflux Pump Regulator

2009 ◽  
Vol 191 (24) ◽  
pp. 7531-7537 ◽  
Author(s):  
Marco Bellinzoni ◽  
Silvia Buroni ◽  
Francis Schaeffer ◽  
Giovanna Riccardi ◽  
Edda De Rossi ◽  
...  
Keyword(s):  
Mycobacterium Smegmatis ◽  
Efflux Pump ◽  
Drug Binding ◽  
Binding Modes ◽  
Transcriptional Repressors ◽  
Gene Encoding ◽  
Drug Binding Site ◽  
Conformational Plasticity ◽  
Local Unfolding ◽  
Calorimetric Studies

ABSTRACT The TetR-like transcriptional repressor LfrR controls the expression of the gene encoding the Mycobacterium smegmatis efflux pump LfrA, which actively extrudes fluoroquinolones, cationic dyes, and anthracyclines from the cell and promotes intrinsic antibiotic resistance. The crystal structure of the apoprotein form of the repressor reveals a structurally asymmetric homodimer exhibiting local unfolding and a blocked drug-binding site, emphasizing the significant conformational plasticity of the protein necessary for DNA and multidrug recognition. Crystallographic and calorimetric studies of LfrR-drug complexes further confirm the intrinsic flexibility of the homodimer, which provides a dynamic mechanism to broaden multidrug binding specificity and may be a general property of transcriptional repressors regulating microbial efflux pump expression.

scholarly journals Phosphorylation-induced unfolding regulates p19INK4dduring the human cell cycle

2018 ◽  
Vol 115 (13) ◽  
pp. 3344-3349 ◽  
Author(s):  
Amit Kumar ◽  
Mohanraj Gopalswamy ◽  
Annika Wolf ◽  
David J. Brockwell ◽  
Mechthild Hatzfeld ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Structural Biology ◽  
Cell Cycle Progression ◽  
S Phase ◽  
Cycle Progression ◽  
Cyclin Dependent Kinases ◽  
Ankyrin Repeat Protein ◽  
Dependent Protein ◽  
Local Unfolding ◽  
Molecular Mode

Cell cycle progression is tightly regulated by cyclin-dependent kinases (CDKs). The ankyrin-repeat protein p19INK4dfunctions as a key regulator of G1/S transition; however, its molecular mode of action is unknown. Here, we combine cell and structural biology methods to unravel the mechanism by which p19INK4dcontrols cell cycle progression. We delineate how the stepwise phosphorylation of p19INK4dSer66 and Ser76 by cell cycle-independent (p38) and -dependent protein kinases (CDK1), respectively, leads to local unfolding of the three N-terminal ankyrin repeats of p19INK4d. This dissociates the CDK6–p19INK4dinhibitory complex and, thereby, activates CDK6. CDK6 triggers entry into S-phase, whereas p19INK4dis ubiquitinated and degraded. Our findings reveal how signaling-dependent p19INK4dunfolding contributes to the irreversibility of G1/S transition.

scholarly journals Targeting and inactivation of bacterial toxins by human defensins

2017 ◽  
Vol 398 (10) ◽  
pp. 1069-1085 ◽  
Author(s):  
Elena Kudryashova ◽  
Stephanie M. Seveau ◽  
Dmitri S. Kudryashov
Keyword(s):  
Innate Immunity ◽  
Structural Similarity ◽  
Fast Response ◽  
Antimicrobial Activities ◽  
Bacterial Toxins ◽  
Host Proteins ◽  
Tertiary Structures ◽  
Local Unfolding ◽  
Human Defensins ◽  
Thermodynamic Instability

Abstract Defensins, as a prominent family of antimicrobial peptides (AMP), are major effectors of the innate immunity with a broad range of immune modulatory and antimicrobial activities. In particular, defensins are the only recognized fast-response molecules that can neutralize a broad range of bacterial toxins, many of which are among the deadliest compounds on the planet. For a decade, the mystery of how a small and structurally conserved group of peptides can neutralize a heterogeneous group of toxins with little to no sequential and structural similarity remained unresolved. Recently, it was found that defensins recognize and target structural plasticity/thermodynamic instability, fundamental physicochemical properties that unite many bacterial toxins and distinguish them from the majority of host proteins. Binding of human defensins promotes local unfolding of the affected toxins, destabilizes their secondary and tertiary structures, increases susceptibility to proteolysis, and leads to their precipitation. While the details of toxin destabilization by defensins remain obscure, here we briefly review properties and activities of bacterial toxins known to be affected by or resilient to defensins, and discuss how recognized features of defensins correlate with the observed inactivation.

Local Unfolding Is Required for the Site-Specific Protein Modification by Transglutaminase

Biochemistry ◽  
2012 ◽  
Vol 51 (43) ◽  
pp. 8679-8689 ◽  
Author(s):  
Barbara Spolaore ◽  
Samanta Raboni ◽  
Amparo Ramos Molina ◽  
Abhijeet Satwekar ◽  
Nunzio Damiano ◽  
...  
Keyword(s):  
Protein Modification ◽  
Specific Protein ◽  
Site Specific ◽  
Local Unfolding

Local Unfolding and Aggregation Mechanisms of SOD1: A Monte Carlo Exploration

2013 ◽  
Vol 117 (31) ◽  
pp. 9194-9202 ◽  
Author(s):  
Anna Bille ◽  
Sigurdur Æ. Jónsson ◽  
Mikael Akke ◽  
Anders Irbäck
Keyword(s):  
Monte Carlo ◽  
Local Unfolding

scholarly journals Global Implications of Local Unfolding Phenomena, Probed by Cysteine Reactivity in Human Frataxin

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Santiago E. Faraj ◽  
Martín E. Noguera ◽  
José María Delfino ◽  
Javier Santos
Keyword(s):  
Local Unfolding
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