tailieunhanh - Báo cáo khoa học: NMR structure of AII in solution compared with the X-ray structure of AII bound to the mAb Fab131

The high-resolution 3D structure of the octapeptide hor-mone angiotensin II (AII) in aqueous solution has been obtained bysimulated annealing calculations, using high-resolutionNMR-derived restraints. After final refinement in explicit water, a familyof 13 structures was obtained with a backbone RMSD of ± A˚ . AII adopts a fairly compact folded structure, with its C-terminus and N-ter-minus approaching towithin A ˚ of eachother. | Eur. J. Biochem. 270 849-860 2003 FEBS 2003 doi On the molecular basis of the recognition of angiotensin II AII NMR structure of AII in solution compared with the X-ray structure of AII bound to the mAb Fab131 Andreas G. Tzakos1. Alexandre M. J. J. Bonvin2. Anasstasios Troaanis3 Paul Cordonatis4 Mario L. Amzel5 . . . . . loannis P. Gerothanassis1 and Nico A. J. van Nuland2 1 Department of Chemistry Section of Organic Chemistry and Biochemistry University of loannina GR-45110 Greece 2Bijvoet Center for Biomolecular Research Department of NMR Spectroscopy Utrecht the Netherlands 3Department of Biological Applications and Technologies University of Ioannina Greece 4Department of Pharmacy University of Patras Greece 5Department of Biophysics and Biophysical Chemistry Johns Hopkins University School of Medicine Baltimore MD 21205 USA The high-resolution 3D structure of the octapeptide hormone angiotensin II AII in aqueous solution has been obtained by simulated annealing calculaiioss. using high-resolution NMR-derived restraints. After final refinement in explicit water a family of 13 sti uctufes was oblaii nedl with a backbone RMSD of A. AII adopts a fairly compact folded structure with its C-terminus and N-ter-minus approaching to within w A of each other. The side chains of Arg2 Tyr4 Ile5 and His6 are oriented on one side of a plane defined by the peptide backbone and the Val3 and Pro7 are pointing in opposite directions. The stabilization of the folded conformation can be explained bythe stacking of the Val3 side chain with the Pro7 ring and by a hedrophobic cluster formed bythe Try4 Ile5 and His6 side chains. Comparison between the NMR-derived structure of AII in aqueous solution and the refined crystal structure of the complex of AII with a high-affinity mAh bub GCircia K. C. Ronco . Verroust . Brunger . Amzel L. M. 1992 Science 257 502-507 provides important quantitative information on two common .