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    • Keywords


      Binding site; interfacial peptides; peptide inhibitor; protein-protein interactions; specific and non-specific interactions

    • Abstract


      An important component of functional genomics involves the understanding of protein association. The interfaces resulting from protein-protein interactions –

      1. specific, as represented by the homodimeric quaternary structures and the complexes formed by two independently occurring protein components, and

      2. 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.

    • Author Affiliations


      Arumay Pal1 Pinak Chakrabarti1 Ranjit Bahadur1 2 Francis Rodier3 Joël Janin2 3

      1. Department of Biochemistry, Bose Institute, P-1/12 CIT Scheme VIIM, Calcutta 700 054, India
      2. Institut de Biochimie et Biologie Moléculaire et Cellulaire, UMR8619 Bât. 430, Université Paris-Sud, 91405-Orsay, France
      3. Laboratoire d’Enzymologie et de Biochimie Structurales, UPR9063 CNRS, 91198-Gif-sur-Yvette, France
    • Dates

  • Journal of Biosciences | News

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      Posted on July 25, 2019

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