BACK TO CONTENTS   |    PDF   |    NEXT

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

 

 

Copyright

 

Publisher

 

 

Copyright Transfer Agreement

 

The authors of published articles in Bioinformation automatically transfer the copyright to the publisher upon formal acceptance. However, the authors reserve right to use the information contained in the article for non commercial purposes.

 

 

 

License

 

This is an open-access article, which permits unrestricted use, distribution, and reproduction in any medium, for non-commercial purposes, provided the original author and source are credited.