BIRCH POLLEN PROFILIN - STRUCTURAL ORGANIZATION AND INTERACTION WITH POLY-(L-PROLINE) PEPTIDES AS REVEALED BY NMR

The secondary structure of birch pollen profilin, a potent human aller gen, was elucidated by multidimensional nuclear magnetic resonance (NM R), as a prerequisite to study the interaction of this profilin with l igands for its poly-(L-proline) (PLP)-binding site, The chemical shift s of the N-15-labeled backbone amide groups were used to monitor compl ex formation with various PLP peptides, Titration with deca-L-proline (P-10) yielded a K-D of 0.2 mM. P-8 was the shortest PLP to provoke a significant reaction, (GP(5))(3)G bound significantly, confirming the interaction between profilins and the protein VASP containing this mot if, Birch profilin interacted also with GP(6)GP(5), found in the cycla se-associated protein (CAP), it suspected profilin ligand. (C) 1997 Fe deration of European Biochemical Societies.