A molecular dynamics study of a model built Pro-36-Gly mutant derived from the potato carboxypeptidase a inhibitor protein

B. Oliva, O. Nilsson, M. Wästlund, R. Cardenas, E. Querol, F. X. Aviès, O. Tapia

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7 Citations (Scopus)

Abstract

A 120ps molecular dynamics (MD) trajectory was calculated and analyzed for a putative Pro36-Gly mutant of the potato carboxypeptidase A (CPA) protein inhibitor (PCIm). The mutant protein's fold shows a large degree of stability, judged from its low α-carbon r.m.s deviation from the X-ray structure of the wild type PCI (PCIw). The N-terminal tail of PCIm differs slightly less from the X-ray structure than it does in PCIw, while the mutant's C-terminal tail (the primary contact site with CPA) and residues 13-17 present deviations as they approach each other. Differences in fluctuation pattern exist between PCIm and PCIw in residues 2-4 (the N-terminal tail), 13-17, 22-23, 28-31 (the secondary contact site with CPA) and 37-38 (the C-terminal tail); the latter region is rigidified in PCIm. Results show that the MD method is able to sense local perturbative effects produced by amino acid substitutions inflexible regions of protein molecules. The simulation suggests that the conformation of the C-terminal tail is less favorable for interaction with the target protein in the mutant than it is in the wild type protein. The Pro-36-Gly mutant is predicted to be a less potent inhibitor. © 1991 Academic Press, Inc.
Original languageEnglish
Pages (from-to)627-632
JournalBiochemical and Biophysical Research Communications
Volume176
Issue number2
DOIs
Publication statusPublished - 30 Apr 1991

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