Optimizing the Photocontrol of bZIP Coiled Coils with Azobenzene Crosslinkers: Role of the Crosslinking Site

ChemBioChem ◽  
2015 ◽  
Vol 16 (12) ◽  
pp. 1757-1763 ◽  
Author(s):  
Ahmed M. Ali ◽  
Matthew W. Forbes ◽  
G. Andrew Woolley
Keyword(s):  
Coiled Coils ◽  
Crosslinking Site

scholarly journals Making or Breaking Metal‐Dependent Catalytic Activity: The Role of Stammers in Designed Three‐Stranded Coiled Coils

2020 ◽  
Vol 132 (46) ◽  
pp. 20625-20629
Author(s):  
Tyler B. J. Pinter ◽  
Elizabeth C. Manickas ◽  
Audrey E. Tolbert ◽  
Karl J. Koebke ◽  
Aniruddha Deb ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Coiled Coils

Unique Role of Clusters of Electrostatic Attractions in Controlling the Stability of Two-stranded α-Helical Coiled-Coils

2009 ◽  
pp. 77-78 ◽  
Author(s):  
J. Paul Kirwan ◽  
Stan C. Kwok ◽  
Susanna McReynolds ◽  
Janine Mills ◽  
David Osguthorpe ◽  
...  
Keyword(s):  
Coiled Coils ◽  
Unique Role ◽  
The Stability

The role of protonation and metal chelation preferences in defining the properties of mercury-binding coiled coils 1 1Edited by P. E. Wright

1998 ◽  
Vol 280 (5) ◽  
pp. 897-912 ◽  
Author(s):  
Gregg R. Dieckmann ◽  
Donald K. McRorie ◽  
James D. Lear ◽  
Kim A. Sharp ◽  
William F. DeGrado ◽  
...  
Keyword(s):  
Coiled Coils ◽  
Metal Chelation

Stable micelles based on a mixture of coiled-coils: the role of different oligomeric states

Nanoscale ◽  
2018 ◽  
Vol 10 (16) ◽  
pp. 7589-7596 ◽  
Author(s):  
Dan Ma ◽  
Sinan Keten
Keyword(s):  
Phase Separation ◽  
Coiled Coils

Phase separation in micelles made up of mixtures of tri- and tetra-meric coiled coils with alkyl and PEG conjugates.

The Role of the N-Terminal Heptad Repeat of HIV-1 in the Actual Lipid Mixing Step as Revealed by Its Substitution with Distant Coiled Coils†

Biochemistry ◽  
2005 ◽  
Vol 44 (15) ◽  
pp. 5853-5861 ◽  
Author(s):  
Yael Wexler-Cohen ◽  
Kelly Sackett ◽  
Yechiel Shai
Keyword(s):  
Coiled Coils ◽  
Heptad Repeat ◽  
Hiv 1

scholarly journals Structural and Functional Analysis of Essential pre-mRNA Splicing Factor Prp19p

2005 ◽  
Vol 25 (1) ◽  
pp. 451-460 ◽  
Author(s):  
Melanie D. Ohi ◽  
Craig W. Vander Kooi ◽  
Joshua A. Rosenberg ◽  
Liping Ren ◽  
Justin P. Hirsch ◽  
...  
Keyword(s):  
Functional Data ◽  
Coiled Coil ◽  
Single Copy ◽  
Coiled Coils ◽  
Binding Partner ◽  
Central Stalk ◽  
Interaction Surface

ABSTRACT U-box-containing Prp19p is an integral component of the Prp19p-associated complex (the nineteen complex, or NTC) that is essential for activation of the spliceosome. Prp19p makes numerous protein-protein contacts with other NTC components and is required for NTC stability. Here we show that Prp19p forms a tetramer in vitro and in vivo and we map the domain required for its oligomerization to a central tetrameric coiled-coil. Biochemical and in vivo analyses are consistent with Prp19p tetramerization providing an interaction surface for a single copy of its binding partner, Cef1p. Electron microscopy showed that the isolated Prp19p tetramer is an elongated particle consisting of four globular WD40 domains held together by a central stalk consisting of four N-terminal U-boxes and four coiled-coils. These structural and functional data provide a basis for understanding the role of Prp19p as a key architectural component of the NTC.

scholarly journals Structure of the merozoite surface protein 1 from Plasmodium falciparum

2021 ◽  
Vol 7 (23) ◽  
pp. eabg0465
Author(s):  
Patricia M. Dijkman ◽  
Tanja Marzluf ◽  
Yingyi Zhang ◽  
Shih-Ying Scott Chang ◽  
Dominic Helm ◽  
...  
Keyword(s):  
Surface Protein ◽  
Merozoite Surface Protein ◽  
Coiled Coils ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Merozoite Surface Protein 1 ◽  
Dimerization Interface ◽  
Structural Insights ◽  
Promising Vaccine Candidate

The merozoite surface protein 1 (MSP-1) is the most abundant protein on the surface of the erythrocyte-invading Plasmodium merozoite, the causative agent of malaria. MSP-1 is essential for merozoite formation, entry into and escape from erythrocytes, and is a promising vaccine candidate. Here, we present monomeric and dimeric structures of full-length MSP-1. MSP-1 adopts an unusual fold with a large central cavity. Its fold includes several coiled-coils and shows structural homology to proteins associated with membrane and cytoskeleton interactions. MSP-1 formed dimers through these domains in a concentration-dependent manner. Dimerization is affected by the presence of the erythrocyte cytoskeleton protein spectrin, which may compete for the dimerization interface. Our work provides structural insights into the possible mode of interaction of MSP-1 with erythrocytes and establishes a framework for future investigations into the role of MSP-1 in Plasmodium infection and immunity.

scholarly journals Separation of coiled-coil structures in lamin A/C is required for elongation of the filament

2020 ◽  
Author(s):  
Jinsook Ahn ◽  
Soyeon Jeong ◽  
So-mi Kang ◽  
Inseong Jo ◽  
Bum-Joon Park ◽  
...  
Keyword(s):  
Structural Transition ◽  
Coiled Coil ◽  
Binding Mode ◽  
Coiled Coils ◽  
Lamin A ◽  
Structural Elements ◽  
Mutant Proteins ◽  
Biochemical Effects ◽  
Insight Into

AbstractIntermediate filaments (IFs) commonly have structural elements of a central α-helical coiled-coil domain consisting of coil 1a, coil 1b, coil 2, and their flanking linkers. Recently, crystal structure of a long lamin A/C fragment was determined and showed detailed features of a tetrameric unit. The structure further suggested a new binding mode between tetramers, designated eA22, where a parallel overlap of coil 1a and coil 2 is the key interaction. In this study, we investigated the biochemical effects of genetic mutations causing human diseases, focusing on the eA22 interaction. The mutant proteins exhibited either weakened or augmented interactions between coil 1a and coil 2. The ensuing biochemical results indicated that the interaction requires the separation of the coiled-coils in N-terminal of coil 1a and C-terminal of coil 2, coupled with the structural transition in the central α-helical rod domain. This study provides insight into the role of coil 1a as a molecular regulator in elongation of the IF proteins.

scholarly journals Essential Role of Coiled Coils for Aggregation and Activity of Q/N-Rich Prions and PolyQ Proteins

Cell ◽  
2010 ◽  
Vol 143 (7) ◽  
pp. 1121-1135 ◽  
Author(s):  
Ferdinando Fiumara ◽  
Luana Fioriti ◽  
Eric R. Kandel ◽  
Wayne A. Hendrickson
Keyword(s):  
Essential Role ◽  
Coiled Coils
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