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BMC Systems Biology
The relationship between domain-domain interaction orientation and sequence similarity Emily Jefferson* and Geoffrey Barton Address: School of Life Sciences, University of Dundee, Dundee, UK Email: Emily Jefferson* - [email protected] * Corresponding author
from BioSysBio 2007: Systems Biology, Bioinformatics and Synthetic Biology Manchester, UK. 11–13 January 2007 Published: 8 May 2007 BMC Systems Biology 2007, 1(Suppl 1):S13
BioSysBio 2007: Systems Biology, Bioinformatics, Synthetic Biology
John Cumbers, Xu Gu, Jong Sze WongMeeting abstracts – A single PDF containing all abstracts in this Supplement is available here.http://www.biomedcentral.com/content/pdf/1752-0509-1-S1-info.pdf
In general proteins of similar sequence have a similar structure. We investigate whether a similar correlation exists between sequence identity and domain-domain interaction similarity. Understanding this relationship is important to the study of many aspects of protein-protein interactions, for example, the prediction of interaction information based on homology to complexes observed in structural data. Here the relationship between sequence identity and interaction similarity is investigated with the inclusion of all interactions within a structure and with redundancy filtering based upon normalisation by the pairwise SCOP  family classification of the interacting domains.
The probability that a pair of interactions were observed at the same orientation was determined and plotted against their sequence identity. The results were normalised by the frequency of the pairwise SCOP  family classification. There is a positive correlation between the probability of the same orientation between a pair of interactions and their % sequence identity (Figure 1).
Materials and methods Domain-domain interactions were employed rather than protein-protein interactions as domains can be considered to be the fundamental functional and structural unit of proteins. SCOP  was chosen as the domain classification system. The domain-domain interactions where again obtained from SNAPPI-DB (Structures, iNterfaces and Alignments of Protein-Protein Interactions – DataBase) . The problem of interactions due to crystal packing artefacts was reduced by use of biological units, as predicted by PQS . Domain-domain interaction orientation was determined using an implementation of the iRMSD method described in Aloy et al . The sequence identity between two domains was obtained from the STAMP  alignment output.
Figure The the same probability 1 orientation that aagainst pair of sequence interactions identity are interacting at The probability that a pair of interactions are interacting at the same orientation against sequence identity.
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BMC Systems Biology 2007, 1(Suppl 1):S13
Conclusion Even at high sequence identities domain-domain interactions have approx. 20% probability of interacting at a different orientation.
Acknowledgements Emily Jefferson is supported by a BBSRC (UK Biotechnology and Biological Sciences Research Council) studentship.
References 1. 2. 3. 4. 5.
Murzin AG, Brenner SE, Hubbard T, Chothia C: SCOP: a structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 1995, 247:536-540. Henrick K, Thornton JM: PQS: a protein quaternary structure file server. Trends Biochem Sci 1998, 23:358-361. Aloy P, Ceulemans H, Stark A, Russell RB: The relationship between sequence and interaction divergence in proteins. J Mol Biol 2003, 332:989-998. Russell RB, Barton GJ: Multiple protein sequence alignment from tertiary structure comparison: assignment of global and residue confidence levels. Proteins 1992, 14:309-323. Jefferson ER, Walsh TP, Barton GJ: SNAPPI-DB: A Database and API of Structures, iNterfaces and Alignments for ProteinProtein Interactions. Nucleic Acids Res in press.
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