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Volume 271, Number 32, Issue of August 9, 1996 pp. 19243-19250
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Secondary Structure and Tertiary Fold of the Birch Pollen Allergen Bet v 1 in Solution

(Received for publication, March 18, 1996, and in revised form, April 25, 1996)

Cornelius Faber , Almut Lindemann , Heinrich Sticht , Andrzej Ejchart , Andreas Kungl ^§ , Markus Susani ^¶ , Rainer W. Frank , Dietrich Kraft ^'' , Michael Breitenbach and Paul Rösch

From  Lehrstuhl für Biopolymere, Universität Bayreuth, Universitätsstr. 30, D-95447 Bayreuth, Germany, ^§ Institut für Genetik und Allgemeine Biologie, Universität Salzburg, A-5020 Salzburg, Austria,   Zentrum für Molekulare Biologie Heidelberg (ZMBH), INF 282, D-69120 Heidelberg, Germany, ^¶ Advanced Biological Systems, Billrothstr. 11, A-5020 Salzburg, Austria, ^§ Sandoz Research Institute, Brunnerstr. 59, A-1235 Wien, Austria, and the ^'' Institut für Allgemeine und Experimentelle Pathologie, Währinger Gürtel 18-20, A-1090 Wien, Austria

Bet v 1 is the major birch pollen allergen and therefore the main cause of type I allergies observed in early spring. It is composed of 159 amino acid residues adding up to a molecular mass of 17 kDa. We determined the secondary structure and tertiary fold of full-length Bet v 1 by NMR spectroscopy. Two- and three-dimensional NMR measurements suggest that Bet v 1 is a globular monomer in solution with a high content of well defined secondary structure. Of the total of 159 residues, 135 could be sequentially assigned, using an improved assignment strategy based mainly on heteronuclear experiments. An improved strategy for structure calculation revealed three helices and two -sheets as major elements of secondary structure. The globular tertiary structure is mainly stabilized by two antiparallel -sheets. The two helices at the C terminus are in accordance with the results from the solution structure of the chemically synthesized peptide Bet v 1-(125-154). This peptide is composed of two helices connected by a hinge. The structural features of Bet v 1 are highly similar to those found in the Ambrosia allergen Amb t V.

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