Birch pollen profilin: structural organization and interaction with poly-( l-proline) peptides as revealed by NMR

• Published in: FEBS letters 1997-07, Vol.411 (2), p.291-295
• Main Authors: Domke, Tobias, Federau, Torsten, Schlüter, Kathrin, Giehl, Klaudia, Valenta, Rudolf, Schomburg, Dietmar, Jockusch, Brigitte M.
• Format: Article
• Language: English
• Subjects: Acanthamoeba - chemistry; Amino Acid Sequence; Animals; Binding Sites; Birch profilin; Cell Adhesion Molecules - metabolism; Cloning, Molecular; Contractile Proteins; Cytoskeletal Proteins; Escherichia coli; Magnetic Resonance Spectroscopy; Microfilament; Microfilament Proteins - chemistry; Microfilament Proteins - metabolism; Molecular Sequence Data; Nuclear magnetic resonance; Peptides - metabolism; Phosphoproteins - metabolism; Plant Proteins - chemistry; Plant Proteins - metabolism; Pollen - chemistry; Poly-( l-proline) motif; Profilins; Protein Binding; Protein Structure, Secondary; Proteins - metabolism; Recombinant Proteins - chemistry; Recombinant Proteins - metabolism; Signal transduction; Trees
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(97)00719-9

The secondary structure of birch pollen profilin, a potent human allergen, was elucidated by multidimensional nuclear magnetic resonance (NMR), as a prerequisite to study the interaction of this profilin with ligands for its poly-( l-proline) (PLP)-binding site. The chemical shifts of the 15N-labeled backbone amide groups were used to monitor complex 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) 3G bound significantly, confirming the interaction between profilins and the protein VASP containing this motif. Birch profilin interacted also with GP 6GP 5, found in the cyclase-associated protein (CAP), a suspected profilin ligand.