02051nam a2200301 a 450000100080000000500110000800800410001910000180006024501480007826001400022650000310036652010370039765000120143465000230144665000110146965300170148065300230149765300310152065300220155165300330157365300310160665300240163770000160166170000150167770000220169270000190171470000160173311913022022-10-24       2008    bl uuuu     u00u1 u    #d1 aTOGAWA, R. C.  aThe table of interface forming residues as the specificity indicator for serine proteases bound to different inhibitors.h[electronic resource]  aIn: INTERNATIONAL CONFERENCE ON BIOINFORMATICS & COMPUTATIONAL BIOLOGY, 2008, Georgia. Las Vegas Nevada: CSREA, 2008, p. 811-817.c2008  aBIOCOMP 2008. WORLDCOMP'08  aWe propose a novel method for defining the exclusive and exhaustive table of serine proteases specificity determining interface forming residues (IFR). The IFR are obtained by "hard body docking" among 73 structurally aligned, sequence wise non redundant, serine protease structures, with 3 inhibitors: ecotine, ovomucoid third domain inhibitor and basic pancreatic trypsin inhibitors. In silico constructed complexes offered a condition for determining which residues are participating, from both enzyme and inhibitor side, in the ensemble of amino acids that upon biding loose contact with a solvent. Our focus is on offering a thorough study on how the specificity is achieved among serine proteases even though they have very little difference in their tertiary structure (specifically if the position of catalytic triad residues is considered). Presented table of serine protease specificity based on IFR position occupation show clear variations among sub families such as: trypsines, chymotrypsines, elastases and thrombines.  aEnzymes  aSerine proteinases  aEnzima  aAminoácidos  aEnzyme specificity  aEspecificidade enzimática  aHard body docking  aInterface formando resíduos  aInterface forming residues  aProteases de serina1 aRIBEIRO, C.1 aMAZONI, I.1 aPELLIGRINELLI, T.1 aJARDINE, J. G.1 aNESHICH, G.