Distinct interfacial biclique patterns between ssDNA-binding proteins and those with dsDNAs

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Journal Article
Proteins: Structure, Function and Bioinformatics, 2011, 79 (2), pp. 598 - 610
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We introduce a new motif called interfacial biclique pattern to study the difference between double-stranded DNA-binding proteins (DSBs, most of them also known to play the role as transcriptional factors) and single-stranded DNA-binding proteins (SSBs) which are found to involve in many applications recently. An interfacial biclique pattern in a protein-DNA complex usually consists of a group of residues and a group of nucleotides such that every residue has a contact to all of the bases. The proposal of this idea is based on a biological redundancy mechanism that: a site mutation has little influence on the other residues to recognize the target nucleotides and vice versa. The distribution of the residues on the interfacial motifs is investigated to identify distinct stable preferred residues, stable un-preferred residues and unstable preferred residues between SSBs and DSBs. We also examine residue co-occurrence and residue-base association rules in the interfacial motifs to uncover the different choices of residue combinations by SSBs and DSBs that have contacts with one or more bases. We found that DSBs and SSBs have their own right residues at the right places for the binding preference and association with nucleotides. Some of our results can be supported by literature work. © 2010 Wiley-Liss, Inc.
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