1G6U

CRYSTAL STRUCTURE OF A DOMAIN SWAPPED DIMER

Summary for 1G6U

• Entry DOI: 10.2210/pdb1g6u/pdb
• Descriptor: DOMAIN SWAPPED DIMER, SULFATE ION, trifluoroacetic acid, ... (4 entities in total)
• Functional Keywords: designed three helix bundle, de novo protein
• Total number of polymer chains: 2
• Total formula weight: 10472.10

Authors

Ogihara, N.L.,Ghirlanda, G.,Bryson, J.W.,Gingery, M.,DeGrado, W.F.,Eisenberg, D. (deposition date: 2000-11-07, release date: 2001-02-21, Last modification date: 2024-02-07)

Primary citation

Ogihara, N.L.,Ghirlanda, G.,Bryson, J.W.,Gingery, M.,DeGrado, W.F.,Eisenberg, D.
Design of three-dimensional domain-swapped dimers and fibrous oligomers.
Proc.Natl.Acad.Sci.USA, 98:1404-1409, 2001

PubMed 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.

PubMed: 11171963
DOI: 10.1073/pnas.98.4.1404

Experimental method

X-RAY DIFFRACTION (1.48 Å)