Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:1.48
Classification:DE NOVO PROTEIN
Release Date:2001-02-21
Deposition Date:2000-11-07
Revision Date:2008-04-27#2011-07-13
Molecular Weight:10472.1
Macromolecule Type:Protein
Residue Count:96
Atom Site Count:728
DOI:10.2210/pdb1g6u/pdb
Abstract:
Three-dimensional (3D) domain-swapped proteins are intermolecularly folded analogs of monomeric proteins; both are stabilized by the identical interactions, but the individual domains interact intramolecularly in monomeric proteins, whereas they form intermolecular interactions in 3D domain-swapped structures. The structures and conditions of formation of several domain-swapped dimers and trimers are known, but the formation of higher order 3D domain-swapped oligomers has been less thoroughly studied. Here we contrast the structural consequences of domain swapping from two designed three-helix bundles: one with an up-down-up topology, and the other with an up-down-down topology. The up-down-up topology gives rise to a domain-swapped dimer whose structure has been determined to 1.5 A resolution by x-ray crystallography. In contrast, the domain-swapped protein with an up-down-down topology forms fibrils as shown by electron microscopy and dynamic light scattering. This demonstrates that design principles can predict the oligomeric state of 3D domain-swapped molecules, which should aid in the design of domain-swapped proteins and biomaterials.
Resolution:1.48
Classification:DE NOVO PROTEIN
Release Date:2001-02-21
Deposition Date:2000-11-07
Revision Date:2008-04-27#2011-07-13
Molecular Weight:10472.1
Macromolecule Type:Protein
Residue Count:96
Atom Site Count:728
DOI:10.2210/pdb1g6u/pdb
Abstract:
Three-dimensional (3D) domain-swapped proteins are intermolecularly folded analogs of monomeric proteins; both are stabilized by the identical interactions, but the individual domains interact intramolecularly in monomeric proteins, whereas they form intermolecular interactions in 3D domain-swapped structures. The structures and conditions of formation of several domain-swapped dimers and trimers are known, but the formation of higher order 3D domain-swapped oligomers has been less thoroughly studied. Here we contrast the structural consequences of domain swapping from two designed three-helix bundles: one with an up-down-up topology, and the other with an up-down-down topology. The up-down-up topology gives rise to a domain-swapped dimer whose structure has been determined to 1.5 A resolution by x-ray crystallography. In contrast, the domain-swapped protein with an up-down-down topology forms fibrils as shown by electron microscopy and dynamic light scattering. This demonstrates that design principles can predict the oligomeric state of 3D domain-swapped molecules, which should aid in the design of domain-swapped proteins and biomaterials.
| Date made available | 2001 |
|---|---|
| Publisher | RCSB-PDB |