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BioMed Research International
Volume 2013 (2013), Article ID 185282, 15 pages
Elucidation of Novel Structural Scaffold in Rohu TLR2 and Its Binding Site Analysis with Peptidoglycan, Lipoteichoic Acid and Zymosan Ligands, and Downstream MyD88 Adaptor Protein
1Fish Health Management Division, Central Institute of Freshwater Aquaculture (CIFA), Kausalyaganga, Bhubaneswar, Odisha 751002, India
2Biomedical Informatics Centre, Rajendra Memorial Research Institute of Medical Sciences, Agamkuan, Patna, Bihar 800007, India
Received 30 March 2013; Revised 10 June 2013; Accepted 11 June 2013
Academic Editor: Claudio M. Soares
Copyright © 2013 Bikash Ranjan Sahoo et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Figure S1. Multiple sequence alignment of rohu TLR2 with other species by MegAlign program. N-termini, C-termini, LRR, trans-membrane (TM) and TIR domain regions are labeled. Conserved residues are shown inside yellow box. Majority axis represents the highest occurrence of a residue in a column.
Figure S2. Ramachandran plot analysis of (a) TLR2-ECD, (b) TLR2-TIR and (c) MyD88-TIR model. The plot was calculated in PROCHECK program.
Figure S3. DIMPLOT analysis of interaction between TLR2-TIR and MyD88-TIR domains (a) HADDOCK analysis and (b) ZDOCK analysis.
Figure S4. The DIMPLOT analysis of TLR2-TIR and MyD88-TIR complex after 10 ns of MDS.
Table S1. Cross-check validation report of homology models.
Table S2. List of predicted binding sites in rohu TLR2-ECD.
Table S3. The predicted interface residues in TLR2-TIR and MyD88-TIR domains.