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Protein Engineering vol. 16 no. 10 pp. 733-738, 2003
© 2003 Oxford University Press

Role of the tyrosine corner motif in the stability of neocarzinostatin

Magali Nicaise1, Marielle Valerio-Lepiniec1, Nadia Izadi-pruneyre2, Elisabeth Adjadj2, Philippe Minard1 and Michel Desmadril1,3

1Laboratoire de Modélisation et d’Ingénierie des Protéines, UMR 8619, Université de Paris-Sud, Bât. 430 and 2Laboratoire de Biophysique Moléculaire, INSERM U 350, Institut Curie, Université de Paris-Sud, Bât 110, F-91405 Orsay Cedex, France M.Nicaise and M.Valerio-Lepiniec contributed equally to this work.

3 To whom correspondence should be addressed. e-mail: michel.desmadril{at}mip.u-psud.fr

Although the immunoglobulin-like ß-sandwich fold has no specifically conserved function, some common structural features have been observed, in particular a structural motif, the tyrosine corner. Such a motif was described in neocarzinostatin (NCS), a bacterial protein the structure of which is very similar to that of the immunoglobulin domain. Compared with the other ß-sheet proteins, the NCS ‘tyrosine corner’ presents non-standard structural features. To investigate the role of this motif in the NCS structure and stability, we studied the properties of a mutant where the H bond interaction had been eliminated by replacing the tyrosine with a phenylalanine. This mutation costs 4.0 kcal/mol showing that the NCS ‘tyrosine corner’ is involved in protein stability as in the other Greek key proteins. This destabilization is accompanied by remote structural effects, including modification of the binding properties, suggesting an increase in the internal flexibility of the protein. With a view to using this protein for drug targeting, these results along with those obtained previously allow us to define clearly the limitations of the modifications that can be performed on this scaffold.

Received December 3, 2002; revised June 6, 2003; accepted September 3, 2003.


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