1ay1
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ANTI TAQ FAB TP7
OverviewOverview
TP7, an antibody against Thermus aquaticus DNA polymerase I (TaqP), is, used as a thermolabile switch in 'hot start' variations of PCR to minimize, non-specific amplification events. Earlier studies have established that, TP7 binds to the polymerase domain of TaqP, competes with primer template, complex for binding and is a potent inhibitor of the polymerase activity, of TaqP. We report crystallographic determination of the structure of an, Fab fragment of TP7 and computational docking of the structure with the, known three-dimensional structure of the enzyme. Our observations strongly, suggest that the origin of inhibitory ability of TP7 is its binding to, enzyme residues involved in DNA binding and polymerization mechanism., Although criteria unbiased by extant biochemical data have been used in, identification of a putative solution, the resulting complex offers an, eminently plausible structural explanation of biochemical observations., The results presented are of general significance for interpretation of, docking experiments and in design of small molecular inhibitors of TaqP, that are not structurally similar to substrates, for use in PCR., Structural and functional similarities noted among DNA polymerases, and, the fact that several DNA polymerases are pharmacological targets, make, discovery of non-substrate based inhibitors of additional importance.
About this StructureAbout this Structure
1AY1 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Structural studies on an inhibitory antibody against Thermus aquaticus DNA polymerase suggest mode of inhibition., Murali R, Helmer-Citterich M, Sharkey DJ, Scalice ER, Daiss JL, Sullivan MA, Krishna Murthy HM, Protein Eng. 1998 Feb;11(2):79-86. PMID:9605541
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