1ay1 | pdb_00001ay1

WARNING: This structure was flagged as problematic. For additional information see 2009, December: at explanation.

ANTI TAQ FAB TP7

spinqualitylabelsall models 1ay1, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ay1 is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Antibody Retractions and Fraud

Proteopedia Page Contributors and Editors (what is this?)

OCA