3D domain swapping
3D domain swapping is a mechanism for forming oligomeric proteins from their monomers. This idea developed from my work as a graduate student in David Eisenberg's lab at UCLA. In 3D domain swapping, one domain of a monomeric protein is
replaced by the same domain from an identical protein chain. The result is
an intertwined dimer or higher oligomer, with one domain of each subunit
replaced by the identical domain from another subunit.
Domain swapping publications
- "3D domain swapping: a mechanism for oligomer assembly and mis-assembly", M.P. Schlunegger, M.J. Bennett and D. Eisenberg (1997). Advances in Protein Chemistry 50 , 61-122.
- "3D domain swapping: a mechanism for oligomer assembly"; Bennett, M.J.,
Schlunegger, M.P. and Eisenberg, D., Protein Science
4, 2455-2468 (1995).
You can read this article in the on-line edition of
Protein Science .
- "Domain swapping: entangling alliances between proteins"; Bennett, M.J.,
Choe, S. and Eisenberg, D., Proc. Natl. Acad. Sci. USA
91, 3127-3131 (1994).