1G6U : CRYSTAL STRUCTURE OF A DOMAIN SWAPPED DIMER

  • David Eisenberg (Contributor)
  • William F. DeGrado (Contributor)
  • Mari Gingery (Contributor)
  • Nancy L. Ogihara (Contributor)
  • Giovanna Ghirlanda (Contributor)
  • Giovanna Ghirlanda (Contributor)
  • James W. Bryson (Contributor)
  • Giovanna Ghirlanda (Contributor)
  • William F. DeGrado (Contributor)

Dataset

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.
Date made availableFeb 21 2001
PublisherRCSB-PDB

Cite this