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This article is part of the supplement: Eighth International Conference on Bioinformatics (InCoB2009): Computational Biology

Open Access Proceedings

Comparative study of protein-protein interaction observed in PolyGalacturonase-Inhibiting Proteins from Phaseolus vulgaris and Glycine max and PolyGalacturonase from Fusarium moniliforme

Aditi Maulik, Hiren Ghosh and Soumalee Basu*

Author Affiliations

Department of Bioinformatics, School of Biotechnology, West Bengal University of Technology BF-142, Salt Lake, Kolkata 700064, India

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BMC Genomics 2009, 10(Suppl 3):S19  doi:10.1186/1471-2164-10-S3-S19

Published: 3 December 2009

Additional files

Additional file 1:

Details of the distribution of the sequence variations in PvPGIP1 and GmPGIP3 with PvPGIP2 over the conserved and variable portion of the repeat and the non-LRR region. The table shows the distribution of the varying residues in PvPGIP1 and GmPGIP3 with PvPGIP2 in the LRRs and non-LRR regions. The changes that occur in the LRR region is either L/N/C of the conserved segment (LxxLxLxxNxL) or is x. They are denoted by cL, cN, cC and cX where X is any amino acid. Amino acid in the variable region of the LRR is denoted by v.

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Additional file 2:

Electrostatic surface potential of PvPGIP2 with a single mutation at 224. Q(224) of PvPGIP2 is mutated to K which is the residue found in PvPGIP1. The electrostatic surface potential changes considerably with a single mutation when compared to Figure 5B. Experimental studies on this single mutation have shown a 70% reduction in the inhibition ability of PvPGIP2.

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Open Data