Title

Protein subunit interfaces: heterodimers versus homodimers

Authors

Cui Zhanhua, Jacob Gah-Kok Gan, Li lei, Meena Kishore Sakharkar, Pandjassarame Kangueane*

Affiliation

School of Mechanical & Aerospace Engineering, Nanyang Technological University, Singapore

E-mail*

mpandjassarame@ntu.edu.sg; * Corresponding author

Article Type

Hypothesis

Date

received July 09, 2005; revised August 05, 2005; accepted August 10, 2005; published online August 11, 2005

Abstract

Protein dimers are either homodimers (complexation of identical monomers) or heterodimers (complexation of non-identical monomers). These dimers are common in catalysis and regulation. However, the molecular principles of protein dimer interactions are difficult to understand mainly due to the geometrical and chemical characteristics of proteins. Nonetheless, the principles of protein dimer interactions are often studied using a dataset of 3D structural complexes determined by X-ray crystallography. A number of physical and chemical properties govern protein dimer interactions. Yet, a handful of such properties are known to dominate protein dimer interfaces. Here, we discuss the differences between homodimer and heterodimer interfaces using a selected set of interface properties.
 

Keywords

Dimer; heterodimer; homodimer; interface; interaction; molecular recognition; interface properties; interface area; hydrogen bonds; hydrophobicity; interface residues

Citation

Zhanhua et al., Bioinformation 1(2): 28-39 (2005)

Edited by

K. Gunasekaran

ISSN

0973-2063

Publisher

Biomedical Informatics

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.