Peptide segments in protein-protein interfaces

Pal, Arumay ; Chakrabarti, Pinak ; Bahadur, Ranjit ; Rodier, Francis ; Janin, Joel (2007) Peptide segments in protein-protein interfaces Journal of Biosciences, 32 (1). pp. 101-111. ISSN 0250-5991

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Official URL: http://www.ias.ac.in/jbiosci/jan2007/101.pdf

Related URL: http://dx.doi.org/10.1007/s12038-007-0010-7

Abstract

An important component of functional genomics involves the understanding of protein association. The interfaces resulting from protein-protein interactions - (i) specific, as represented by the homodimeric quaternary structures and the complexes formed by two independently occurring protein components, and (ii) non-specific, as observed in the crystal lattice of monomeric proteins - have been analysed on the basis of the length and the number of peptide segments. In 1000 Å2 of the interface area, contributed by a polypeptide chain, there would be 3.4 segments in homodimers, 5.6 in complexes and 6.3 in crystal contacts. Concomitantly, the segments are the longest (with 8.7 interface residues) in homodimers. Core segments (likely to contribute more towards binding) are more in number in homodimers (1.7) than in crystal contacts (0.5), and this number can be used as one of the parameters to distinguish between the two types of interfaces. Dominant segments involved in specific interactions, along with their secondary structural features, are enumerated.

Item Type:Article
Source:Copyright of this article belongs to Indian Academy of Sciences.
Keywords:Binding Site; Interfacial Peptides; Peptide Inhibitor; Protein-protein Interactions; Specific and Non-specific Interactions
ID Code:89219
Deposited On:24 Apr 2012 12:38
Last Modified:19 May 2016 03:48

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