Active Monomeric and Dimeric Forms ofPseudomonas putidaGlyoxalase I:  Evidence for 3D Domain Swapping†

Biochemistry ◽  
1998 ◽  
Vol 37 (29) ◽  
pp. 10345-10353 ◽  
Author(s):  
André P. Saint-Jean ◽  
Kristina R. Phillips ◽  
Donald J. Creighton ◽  
Martin J. Stone
Keyword(s):  
Domain Swapping

Protein Reconstitution and 3D Domain Swapping

2002 ◽  
Vol 3 (6) ◽  
pp. 629-642 ◽  
Author(s):  
Maria Hakansson ◽  
Sara Linse
Keyword(s):  
Domain Swapping ◽  
Protein Reconstitution

scholarly journals Interactions Crucial for Three-Dimensional Domain Swapping in the HP-RNase Variant PM8

2011 ◽  
Vol 101 (2) ◽  
pp. 459-467 ◽  
Author(s):  
Pere Tubert ◽  
Douglas V. Laurents ◽  
Marc Ribó ◽  
Marta Bruix ◽  
Maria Vilanova ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Domain Swapping ◽  
Dimensional Domain

scholarly journals 3D Domain Swapping Modulates the Stability of Members of an Icosahedral Virus Group

Structure ◽  
2000 ◽  
Vol 8 (10) ◽  
pp. 1095-1103 ◽  
Author(s):  
Chunxu Qu ◽  
Lars Liljas ◽  
Natacha Opalka ◽  
Christophe Brugidou ◽  
Mark Yeager ◽  
...  
Keyword(s):  
Domain Swapping ◽  
Virus Group ◽  
Icosahedral Virus ◽  
The Stability

scholarly journals Small Molecule-Induced Domain Swapping as a Mechanism for Controlling Protein Function and Assembly

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Joshua M. Karchin ◽  
Jeung-Hoi Ha ◽  
Kevin E. Namitz ◽  
Michael S. Cosgrove ◽  
Stewart N. Loh
Keyword(s):  
Small Molecule ◽  
Protein Function ◽  
Domain Swapping

scholarly journals Stabilization, Characterization, and Selective Removal of Cystatin C Amyloid Oligomers

2013 ◽  
Vol 288 (23) ◽  
pp. 16438-16450 ◽  
Author(s):  
Gustav Östner ◽  
Veronica Lindström ◽  
Per Hjort Christensen ◽  
Maciej Kozak ◽  
Magnus Abrahamson ◽  
...  
Keyword(s):  
Cystatin C ◽  
Amyloid Fibrils ◽  
Dynamic Equilibrium ◽  
Biological Fluids ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Domain Swapping ◽  
Amyloid Angiopathy ◽  
Force Microscopy ◽  
And Function

The pathophysiological process in amyloid disorders usually involves the transformation of a functional monomeric protein via potentially toxic oligomers into amyloid fibrils. The structure and properties of the intermediary oligomers have been difficult to study due to their instability and dynamic equilibrium with smaller and larger species. In hereditary cystatin C amyloid angiopathy, a cystatin C variant is deposited in arterial walls and cause brain hemorrhage in young adults. In the present investigation, we use redox experiments of monomeric cystatin C, stabilized against domain swapping by an intramolecular disulfide bond, to generate stable oligomers (dimers, trimers, tetramers, decamers, and high molecular weight oligomers). These oligomers were characterized concerning size by gel filtration, polyacrylamide gel electrophoresis, and mass spectrometry, shape by electron and atomic force microscopy, and, function by assays of their capacity to inhibit proteases. The results showed the oligomers to be highly ordered, domain-swapped assemblies of cystatin C and that the oligomers could not build larger oligomers, or fibrils, without domain swapping. The stabilized oligomers were used to induce antibody formation in rabbits. After immunosorption, using immobilized monomeric cystatin C, and elution from columns with immobilized cystatin C oligomers, oligomer-specific antibodies were obtained. These could be used to selectively remove cystatin C dimers from biological fluids containing both dimers and monomers.

scholarly journals Domain swapping is a consequence of minimal frustration

2004 ◽  
Vol 101 (38) ◽  
pp. 13786-13791 ◽  
Author(s):  
S. Yang ◽  
S. S. Cho ◽  
Y. Levy ◽  
M. S. Cheung ◽  
H. Levine ◽  
...  
Keyword(s):  
Domain Swapping

scholarly journals TADOSS: computational estimation of tandem domain swap stability

2018 ◽  
Vol 35 (14) ◽  
pp. 2507-2508 ◽  
Author(s):  
Aleix Lafita ◽  
Pengfei Tian ◽  
Robert B Best ◽  
Alex Bateman
Keyword(s):  
Large Scale ◽  
Domain Swapping ◽  
Coarse Grained ◽  
Supplementary Information ◽  
Simulation Studies ◽  
Computational Tools ◽  
Domain Swap ◽  
Computational Estimation ◽  
High Propensity ◽  
The Stability

Abstract Summary Proteins with highly similar tandem domains have shown an increased propensity for misfolding and aggregation. Several molecular explanations have been put forward, such as swapping of adjacent domains, but there is a lack of computational tools to systematically analyze them. We present the TAndem DOmain Swap Stability predictor (TADOSS), a method to computationally estimate the stability of tandem domain-swapped conformations from the structures of single domains, based on previous coarse-grained simulation studies. The tool is able to discriminate domains susceptible to domain swapping and to identify structural regions with high propensity to form hinge loops. TADOSS is a scalable method and suitable for large scale analyses. Availability and implementation Source code and documentation are freely available under an MIT license on GitHub at https://github.com/lafita/tadoss. Supplementary information Supplementary data are available at Bioinformatics online.

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