Results 11 to 20 of about 83,637 (272)

3D domain swapping: As domains continue to swap [PDF]

open access: yesProtein Science, 2002
Abstract Three‐dimensional (3D) domain swapping creates a bond between two or more protein molecules as they exchange their identical domains. Since the term '3D domain swapping' was first used to describe the dimeric structure of diphtheria toxin, the database of domain‐swapped proteins has greatly expanded. Analyses of the now about
Yanshun, Liu, David, Eisenberg
openaire   +4 more sources

Domain swapping and amyloid fibril conformation [PDF]

open access: yesPrion, 2012
For several different proteins an apparent correlation has been observed between the propensity for dimerization by domain-swapping and the ability to aggregate into amyloid-like fibrils.
Van Der Wel, PCA
core   +4 more sources

Deposition Diseases and 3D Domain Swapping [PDF]

open access: yesStructure, 2006
Protein aggregation is a feature of both normal cellular assemblies and pathological protein depositions. Although the limited order of aggregates has often impeded their structural characterization, 3D domain swapping has been implicated in the formation of several protein aggregates.
Bennett, Melanie J.   +2 more
openaire   +4 more sources

Domain swapping in allosteric modulation of DNA specificity.

open access: yesPLoS Biology, 2010
SgrAI is a type IIF restriction endonuclease that cuts an unusually long recognition sequence and exhibits allosteric self-modulation of cleavage activity and sequence specificity.
Chad K Park   +7 more
doaj   +3 more sources

3D domain swapping: A mechanism for oligomer assembly [PDF]

open access: yesProtein Science, 1995
Abstract3D domain swapping is a mechanism for forming oligomeric proteins from their monomers. In 3D domain swapping, one domain of a monomeric protein is replaced by the same domain from an identical protein chain. The result is an intertwined dimer or higher oligomer, with one domain of each subunit replaced by the identical domain from another ...
M J, Bennett   +2 more
openaire   +4 more sources

Regulation of Dishevelled DEP domain swapping by conserved phosphorylation sites. [PDF]

open access: yesProc Natl Acad Sci U S A, 2021
Beitia GJ   +5 more
europepmc   +2 more sources

Domain Swapping and Retroviral Assembly [PDF]

open access: yesMolecular Cell, 2005
The structure of a mammalian SCAN domain has been recently reported. The molecule is a structural homolog of the HIV-1 capsid protein and forms a domain-swapped dimer in solution. The authors propose a similar domain-swapping event facilitates HIV-1 assembly, providing a new model for protein-protein interactions underlying viral particle formation.
Kingston, Richard L., Vogt, Volker M.
openaire   +2 more sources

Topological Determinants of Protein Domain Swapping [PDF]

open access: yesStructure, 2006
Protein domain swapping has been repeatedly observed in a variety of proteins and is believed to result from destabilization due to mutations or changes in environment. Based on results from our studies and others, we propose that structures of the domain-swapped proteins are mainly determined by their native topologies. We performed molecular dynamics
Ding, Feng   +3 more
openaire   +2 more sources

Unraveling the Functional Significance of Unstructured Regions in G Protein-Coupled Receptors

open access: yesBiomolecules, 2023
Unstructured regions in functional proteins have gained attention in recent years due to advancements in informatics tools and biophysical methods.
Roberto Maggio   +5 more
doaj   +1 more source

Dramatic structural changes resulting from the loss of a crucial hydrogen bond in the hinge region involved in C-terminal helix swapping in SurE: a survival protein from Salmonella typhimurium. [PDF]

open access: yesPLoS ONE, 2013
Domain swapping is an interesting feature of some oligomeric proteins in which each protomer of the oligomer provides an identical surface for exclusive interaction with a segment or domain belonging to another protomer.
Yamuna Kalyani Mathiharan   +3 more
doaj   +1 more source

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