The importance of being dimeric
- 2 December 2004
- journal article
- review article
- Published by Wiley in The FEBS Journal
- Vol. 272 (1) , 16-27
- https://doi.org/10.1111/j.1432-1033.2004.04407.x
Abstract
Why are there so many dimeric proteins and enzymes? While for heterodimers a functional explanation seems quite reasonable, the case of homodimers is more puzzling. The number of homodimers found in all living organisms is rapidly increasing. A thorough inspection of the structural data from the available literature and stability (measured from denaturation–renaturation experiments) allows one to suggest that homodimers can be divided into three main types according to their mass and the presence of a (relatively) stable monomeric intermediate in the folding–unfolding pathway. Among other explanations, we propose that an essential advantage for a protein being dimeric may be the proper and rapid assembly in the cellular milieu.Keywords
This publication has 64 references indexed in Scilit:
- Stability of a homo-dimeric Ca2+-binding member of the βγ-crystallin superfamily: DSC measurements on spherulin 3a from Physarum polycephalumJournal of Molecular Biology, 1999
- Contact order, transition state placement and the refolding rates of single domain proteins 1 1Edited by P. E. WrightJournal of Molecular Biology, 1998
- A folded monomeric intermediate in the formation of lambda cro dimer-dNA complexesJournal of Molecular Biology, 1997
- Characterization of Charge Change Super-repressor Mutants oftrpRepressor: Effects on Oligomerization Conformation, Ligation and StabilityJournal of Molecular Biology, 1996
- Three hTIM Mutants that Provide New Insights on why TIM is a DimerJournal of Molecular Biology, 1996
- Equilibrium dissociation and unfolding of the dimeric human papillomavirus strain‐16 E2 DNA‐binding domainProtein Science, 1996
- Unfolding of 4-aminobutyrate aminotransferase equilibrium and kinetic studiesBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1994
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982
- Protein Shape and Biological ControlScientific American, 1973
- On the nature of allosteric transitions: A plausible modelJournal of Molecular Biology, 1965