Title

Insights from the structural analysis of protein heterodimer interfaces 

Authors

Gopichandran Sowmya^{1, 2}*, Sathyanarayanan Anita², Pandjassarame Kangueane^{1, 2} 

Affiliation

¹Department of Biotechnology, Faculty of applied Science, AIMST University, 08100 Semeling, Malaysia; ²Biomedical Informatics, Pondicherry 607402, India

Email

sowmyagopichandran@gmail.com; *Corresponding author

Phone

+914132633589

Fax

+914132633722

Article Type

Hypothesis

Date

Received April 15, 2011; Accepted May 07, 2011; Published May 07, 2011
 

Protein heterodimer complexes are often involved in catalysis, regulation, assembly, immunity and inhibition. This involves the formation of stable interfaces between the interacting partners. Hence, it is of interest to describe heterodimer interfaces using known structural complexes. We use a non-redundant dataset of 192 heterodimer complex structures from the protein databank (PDB) to identify interface residues and describe their interfaces using amino-acids residue property preference. Analysis of the dataset shows that the heterodimer interfaces are often abundant in polar residues. The analysis also shows the presence of two classes of interfaces in heterodimer complexes. The first class of interfaces (class A) with more polar residues than core but less than surface is known. These interfaces are more hydrophobic than surfaces, where protein-protein binding is largely hydrophobic. The second class of interfaces (class B) with more polar residues than core and surface is shown. These interfaces are more polar than surfaces, where binding is mainly polar. Thus, these findings provide insights to the understanding of protein-protein interactions. 

Keywords

protein-protein interaction (PPI); heterodimer; interface; surface; core; polar abundance.
 

Citation

Sowmya et al. Bioinformation 6(4): 137-143(2011)

Edited by

VS Mathura

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.