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- W1590313270 abstract "Publisher Summary This chapter examines one type of interchain, noncovalent protein-protein bond: 3D domain swapping. To date, 3D domain swapping has been definitively established only in closed oligomers and seen in crystallographic detail only in dimeric proteins. The extent and significance of 3D domain swapping in functional and malfunctional protein assemblies are explored. The tendency of a protein to undergo 3D domain swapping is governed by structural, thermodynamic, and kinetic factors. Structural factors are considered in the following section; thermodynamic and kinetic factors are discussed here, which has specific features for diphtheria toxin but also general features that apply to all 3D domain swapped proteins. The thermodynamic and kinetic factors that govern 3D domain swapping are influenced by the amino acid sequence and three-dimensional structure of the protein, which in turn are affected by mutations. The most critical factor is that the protein contains a segment of polypeptide chain that can act as a hinge loop. The role of amino acid sequence and three-dimensional structure in 3D domain swapping is discussed. The chapter closes with a brief consideration of the possibility that 3D domain swapping is a mechanism for the formation of amyloid or other pathological aggregates of proteins." @default.
- W1590313270 created "2016-06-24" @default.
- W1590313270 creator A5034709520 @default.
- W1590313270 creator A5068436282 @default.
- W1590313270 creator A5080439570 @default.
- W1590313270 date "1997-01-01" @default.
- W1590313270 modified "2023-10-10" @default.
- W1590313270 title "Oligomer Formation By 3D Domain Swapping: A Model For Protein Assembly And Misassembly" @default.
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