3D domain swapping: Structural characterizations of domain-swapped dimer proteins FVE and rhodocetin

Abstract

The phenomenon of 3-D domain swapping has been studied by examining: (1) bona fide 3-D domain-swapped proteins, the structures of whose monomeric and oligomeric forms have been characterized by X-ray diffraction or NMR, (2) pairs of proteins whose structures mimic monomeric and 3-D domain-swapped oligomers, but whose amino acid sequences differ, and (3) intertwined oligomers that are reminiscent of 3-D domain-swapped proteins, but for which no monomeric form is known. The structure of the Fve falls into the last category of candidate for 3D domain swapping, since the monomer is not known while, the rhodocetin falls into second category , if MBP is taken as the reference monomer as described for IX/X-bp.