1ql9
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FACTOR XA SPECIFIC INHIBITOR IN COMPLEX WITH RAT TRYPSIN MUTANT X99RT
OverviewOverview
In order to investigate issues of selectivity and specificity in, protein-ligand interactions, we have undertaken the reconstruction of the, binding pocket of human factor Xa in the structurally related rat trypsin, by site-directed mutagenesis. Three sequential regions (the "99"-, the, "175"- and the "190"- loops) were selected as representing the major, structural differences between the ligand binding sites of the two, enzymes. Wild-type rat trypsin and variants X99rT and X(99/175/190)rT were, expressed in yeast, and analysed for their interaction with factor Xa and, trypsin inhibitors. For most of the inhibitors studied, progressive loop, replacement at the trypsin surface resulted in inhibitory profiles akin to, factor Xa. Crystals of the variants were obtained in the presence of, ... [(full description)]
About this StructureAbout this Structure
1QL9 is a [Single protein] structure of sequence from [Rattus norvegicus] with CA, SO4 and ZEN as [ligands]. Active as [Trypsin], with EC number [3.4.21.4]. Structure known Active Sites: AC1, AC2, AC3 and ACT. Full crystallographic information is available from [OCA].
ReferenceReference
Reconstructing the binding site of factor Xa in trypsin reveals ligand-induced structural plasticity., Reyda S, Sohn C, Klebe G, Rall K, Ullmann D, Jakubke HD, Stubbs MT, J Mol Biol. 2003 Jan 31;325(5):963-77. PMID:12527302
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