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CORRECTION

Protein Science 16: 14–19 (2007)

Solution structure of a small protein containing a fluorinated side chain in the core

Gabriel Cornilescu, Erik B. Hadley, Matthew G. Woll, John L. Markley, Samuel H. Gellman, and Claudia C. Cornilescu

We, the authors, retract the claim that the structure reported is the first to include a fluorinated side chain. A number of prior structures that contain side chains bearing a single H F substitution have been reported, and we regret not having cited these (Ji et al. 1994, 1997; Xiao et al. 1998; Minks et al. 1999; Rozovsky et al. 2001; Campos-Olivas et al. 2002; Alexeev et al. 2003; Bae et al. 2004; Ayala et al. 2005; Wang et al. 2005). To our knowledge, however, ours is the first report of a protein structure containing a more heavily fluorinated side chain (bearing at least three F atoms), for which non-negligible structural rearrangements may be expected.

	References

TOP References

 
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Ayala, I., Perry, J.J., Szczepanski, J., Tainer, J.A., Vala, M.T., Nick, H.S., and Silverman, D.N. 2005. Hydrogen bonding in human manganese superoxide dismutase containing 3-fluorotyrosine. Biophys. J. 89: 4171–4179.[CrossRef][Medline]

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Campos-Olivas, R., Aziz, R., Helms, G.L., Evans, J.N.S., and Gronenborn, A.M. 2002. Placement of 19F into the center of GB1: Effects on structure and stability. FEBS Letters 517: 55–60.[CrossRef][Medline]

Ji, X.H., Johnson, W.W., Sesay, M.A., Dickert, L., Prasad, S.M., Ammon, H.L., Armstrong, R.N., and Gilliland, G.L. 1994. Structure and function of the xenobiotic substrate-binding site of A glutathione-S-transferase as revealed by X-ray crystallographic analysis of product complexes with diastereomers of 9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene. Biochem. 33: 1043–1052.[CrossRef][Medline]

Ji, X.H., Tordova, M., O'Donnell, R., Parsons, J.F., Hayden, J.B., Gilliland, G.L., and Zimniak, P. 1997. Structure and function of the xenobiotic substrate-binding site and location of a potential non-substrate-binding site in a class pi glutathione S-transferase. Biochem. 36: 9690–9702.[CrossRef][Medline]

Minks, C., Huber, R., Moroder, L., and Budisa, N. 1999. Atomic mutations at the single tryptophan residue of human recombinant annexin V: Effects on structure, stability, and activity. Biochem. 38: 10649–10659.[CrossRef][Medline]

Rozovsky, S., Jogl, G., Tong, L., and McDermott, A.E. 2001. Solution-state NMR investigations of triosephosphate isomerase active site loop motion: Ligand release in relation to active site loop dynamics. J. Mol. Biol. 310: 271–280.[CrossRef][Medline]

Wang, X., Mercier, P., Letourneau, P.J., and Sykes, B.D. 2005. Effects of Phe-to-Trp mutation and fluorotryptophan incorporation on the solution structure of cardiac troponin C, and analysis of its suitability as a potential probe for in situ NMR studies. Protein Sci. 14: 2447–2460.[Abstract/Free Full Text]

Xiao, G.Y., Parsons, J.F., Tesh, K., Armstrong, R.N., and Gilliland, G.L. 1998. Conformational changes in the crystal structure of rat glutathione transferase M1-1 with global substitution of 3-flurortyrosine for tyrosine. J. Mol. Biol. 281: 323–339.[CrossRef][Medline]

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This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                   What's this?