By Ivan Mura (auth.), Luis F. Castillo, Marco Cristancho, Gustavo Isaza, Andrés Pinzón, Juan Manuel Corchado Rodríguez (eds.)
This quantity compiles permitted contributions for the second version of the Colombian Computational Biology and Bioinformatics Congress CCBCOL, after a rigorous assessment procedure within which fifty four papers have been approved for book from 119 submitted contributions. Bioinformatics and Computational Biology are components of information that experience emerged as a result of advances that experience taken position within the organic Sciences and its integration with info Sciences. the growth of initiatives related to the learn of genomes has led the way in which within the construction of gigantic quantities of series facts which should be prepared, analyzed and kept to appreciate phenomena linked to residing organisms concerning their evolution, habit in several ecosystems, and the improvement of functions that may be derived from this analysis.
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Extra info for Advances in Computational Biology: Proceedings of the 2nd Colombian Congress on Computational Biology and Bioinformatics (CCBCOL)
PDGF-B binding to the EGFR. Interaction between TYR 42 (EGFR) and ILE E 13 E 13 (PDGF-B chain A). 3 Å. by polar contact (yellow dotted 14, THR 15, TRP 40, TYR R 45, ASN 151, LYS 81, ARG 125, LEU 69, TYR 1101, PHE 84. ARG 73, LYS 105, GLN 71, SER92, GLU90, ASN91, PRO82, ILE77. Results show that SER 127, ASP A 155, LYS 86, LYS 81, ASN 151, GLN 71 and L LYS 105 are present in the hydrogen bond formation within this complex, suggesting the importance of both hydrop phobic interactions and hydrogen bond for the bindingg of PDGF-BB to EGFR.
Interestingly, in the present study, we have reported ILE13, ARG73, ILE77, LYS 81, PRO82 and PHE84, as part of the binding interactions between PDGF-BB and EGFR. These results suggests a possible conserved motif in the interaction between PDGFB and EGFR which could be important in the binding of PDGF-BB with other receptors such as PDGFRα, that can associate with PDGFRβ and form the heterodimeric PDGFRαβ. It has been previously reported that both hydrophobic interactions and hydrogen bonds play an important role in the recognition of the PDGFR to its ligand , Our results show that both of these interactions are important for the binding interaction of PDGF-BB to EGFR.
Neurosci. 16(6), 748–754 (2009) 4. : On the tertiary structure of the extracellular domains of the epidermal growth factor and insulin receptors. Biochim. Bio. Phys. Acta. 916, 220–226 (1987) 5. : Insulin and epidermal growth factor receptors contain the cysteine repeat motif found in the tumor necrosis factor receptor. Proteins 22, 141–153 (1995) 38 R. Cabezas et al. 6. : Structural evidence for loose linkage between ligand binding and kinase activation in the epidermal growth factor receptor.
Advances in Computational Biology: Proceedings of the 2nd Colombian Congress on Computational Biology and Bioinformatics (CCBCOL) by Ivan Mura (auth.), Luis F. Castillo, Marco Cristancho, Gustavo Isaza, Andrés Pinzón, Juan Manuel Corchado Rodríguez (eds.)