scholarly journals Structural Insights into the Intrinsic Self-Assembly of Par-3 N-Terminal Domain

Structure ◽  
2013 ◽  
Vol 21 (6) ◽  
pp. 997-1006 ◽  
Author(s):  
Yan Zhang ◽  
Wenjuan Wang ◽  
Jia Chen ◽  
Kai Zhang ◽  
Feng Gao ◽  
...  
Keyword(s):  
Self Assembly ◽  
Terminal Domain ◽  
Structural Insights

Structural insights into the transient closed conformation and pH dependent ATPase activity of S.Typhi GyraseB N- terminal domain

2021 ◽  
Vol 701 ◽  
pp. 108786
Author(s):  
Deepali Gupta ◽  
Pragya Tiwari ◽  
Md Anzarul Haque ◽  
Ekta Sachdeva ◽  
Md Imtaiyaz Hassan ◽  
...  
Keyword(s):  
Atpase Activity ◽  
Closed Conformation ◽  
Terminal Domain ◽  
Dependent Atpase ◽  
Ph Dependent ◽  
Structural Insights

scholarly journals Quantification of amyloid fibril polymorphism by nano-morphometry reveals the individuality of filament assembly

2020 ◽  
Vol 3 (1) ◽  
Author(s):  
Liam D. Aubrey ◽  
Ben J. F. Blakeman ◽  
Liisa Lutter ◽  
Christopher J. Serpell ◽  
Mick F. Tuite ◽  
...  
Keyword(s):  
Self Assembly ◽  
Amyloid Fibrils ◽  
Amyloid Fibril ◽  
Biological Function ◽  
Structural Basis ◽  
Distance Curve ◽  
Filament Assembly ◽  
Sample Heterogeneity ◽  
Structural Insights ◽  
Polymorphic Nature

Abstract Amyloid fibrils are highly polymorphic structures formed by many different proteins. They provide biological function but also abnormally accumulate in numerous human diseases. The physicochemical principles of amyloid polymorphism are not understood due to lack of structural insights at the single-fibril level. To identify and classify different fibril polymorphs and to quantify the level of heterogeneity is essential to decipher the precise links between amyloid structures and their functional and disease associated properties such as toxicity, strains, propagation and spreading. Employing gentle, force-distance curve-based AFM, we produce detailed images, from which the 3D reconstruction of individual filaments in heterogeneous amyloid samples is achieved. Distinctive fibril polymorphs are then classified by hierarchical clustering, and sample heterogeneity is objectively quantified. These data demonstrate the polymorphic nature of fibril populations, provide important information regarding the energy landscape of amyloid self-assembly, and offer quantitative insights into the structural basis of polymorphism in amyloid populations.

scholarly journals Preliminary X-ray crystallographic analysis of an engineered variant of human chimera-type galectin-3 with a shortened N-terminal domain

2015 ◽  
Vol 71 (2) ◽  
pp. 184-188 ◽  
Author(s):  
Andrea Flores-Ibarra ◽  
Federico M. Ruiz ◽  
Sabine Vértesy ◽  
Sabine André ◽  
Hans-Joachim Gabius ◽  
...  
Keyword(s):  
Crystallographic Analysis ◽  
Modular Organization ◽  
Unit Cell Parameters ◽  
Orthorhombic Space Group ◽  
X Ray ◽  
Cell Parameters ◽  
Cellular Effects ◽  
Terminal Domain ◽  
Galectin 3 ◽  
Structural Insights

How lectins translate sugar-encoded information into cellular effects not only depends on glycan recognition. Other domains of the protein can contribute to the functional profile of a lectin. Human galectin-3 (Gal-3), an adhesion/growth-regulatory galectin, is composed of three different domains and is thus called a chimera-type protein. In addition to the carbohydrate-recognition domain, this lectin encompasses an N-terminal domain consisting of a peptide harbouring two phosphorylation sites and nine non-triple-helical collagen-like repeats. This region plays an as yet structurally undefined role in Gal-3 aggregation and ligand recognition. To date, crystallization of full-length Gal-3 has not been achieved. With the aim of providing structural insights into this modular organization, a Gal-3 variant was crystallized maintaining the terminal peptide and three of the nine collagen-like repeats. The crystals belonged to the orthorhombic space groupP212121, with unit-cell parametersa= 94.04,b= 97.96,c= 236.20 Å, and diffracted to a resolution of 3.3 Å.

Extractant mediated nano-aggregate formation in Triton X-114 aided cloud formation: structural insights from TEM and SANS studies

RSC Advances ◽  
2015 ◽  
Vol 5 (116) ◽  
pp. 95613-95617 ◽  
Author(s):  
N. Kumari ◽  
P. K. Verma ◽  
P. N. Pathak ◽  
A. Gupta ◽  
A. Ballal ◽  
...  
Keyword(s):  
Self Assembly ◽  
Tributyl Phosphate ◽  
Cloud Formation ◽  
Aggregate Formation ◽  
Triton X ◽  
Structural Insights

Nanoaggregate formation by self assembly was noticed during the cloud formation of Triton X-114 in the presence of dibenzoylmethane (DBM), thenoyltrifluoroacetone (HTTA) and 1-phenyl-3-methyl-4-benzoyl-5-pyrazolone (PMBP) and tributyl phosphate (TBP).

scholarly journals Structural insights into peptide self‐assembly using photo‐induced crosslinking experiments and discontinuous molecular dynamics

AIChE Journal ◽  
2020 ◽  
Author(s):  
Samuel J. Bunce ◽  
Yiming Wang ◽  
Sheena E. Radford ◽  
Andrew J. Wilson ◽  
Carol K. Hall
Keyword(s):  
Molecular Dynamics ◽  
Self Assembly ◽  
Structural Insights

scholarly journals Spidroin N-terminal Domain Promotes a pH-dependent Association of Silk Proteins during Self-assembly

2010 ◽  
Vol 285 (52) ◽  
pp. 40745-40753 ◽  
Author(s):  
William A. Gaines ◽  
Michael G. Sehorn ◽  
William R. Marcotte
Keyword(s):  
Self Assembly ◽  
Silk Proteins ◽  
Terminal Domain ◽  
Ph Dependent

scholarly journals Structural characterization of the N-terminal domain of the Dictyostelium discoideum mitochondrial calcium uniporter

2019 ◽  
Author(s):  
Yuan Yuan ◽  
Chan Cao ◽  
Maorong Wen ◽  
Min Li ◽  
Ying Dong ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Dictyostelium Discoideum ◽  
Self Assembly ◽  
Calcium Influx ◽  
Transmembrane Protein ◽  
Critical Role ◽  
Mitochondrial Calcium ◽  
Mitochondrial Calcium Uniporter ◽  
Terminal Domain ◽  
Calcium Uniporter

AbstractThe mitochondrial calcium uniporter (MCU) plays a critical role in the mitochondrial calcium uptake into the matrix. In metazoans, the uniporter is a tightly regulated multi-component system including the pore-forming subunit MCU and several regulators (MICU1, MICU2, EMRE). The calcium-conducting activity of metazoan MCU requires the single-transmembrane protein EMRE. Dictyostelium discoideum (Dd), however, developed a simplified uniporter for which the pore-forming MCU (DdMCU) alone is necessary and sufficient for calcium influx. Here, we report a crystal structure of the N-terminal domain (NTD) of DdMCU at 1.7 Å resolution. The DdMCU-NTD contains four helices and two strands arranged in a fold that is completely different from the known structures of other MCU-NTD homologs. Biochemical and biophysical analyses of DdMCU-NTD in solution indicated that the domain exists as oligomers, most probably as a pentamer or hexamer. Mutagenesis showed that the acidic residues Asp60, Glu72 and Glu74, which appeared to mediate the parallel interface as observed in the crystal structure, participated in the self-assembly of DdMCU-NTD. Intriguingly, the oligomeric complex readily dissociated to lower-order oligomers in the presence of calcium. We propose that the calcium-triggered dissociation of NTD regulates the channel activity of DdMCU by a yet unknown mechanism.

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