Birch pollen profilin: structural organization and interaction with poly‐(l‐proline) peptides as revealed by NMR
Open Access
- 14 July 1997
- journal article
- Published by Wiley in FEBS Letters
- Vol. 411 (2-3) , 291-295
- https://doi.org/10.1016/s0014-5793(97)00719-9
Abstract
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 (P10) yielded a K D of 0.2 mM. P8 was the shortest PLP to provoke a significant reaction. (GP5)3G bound significantly, confirming the interaction between profilins and the protein VASP containing this motif. Birch profilin interacted also with GP6GP5, found in the cyclase‐associated protein (CAP), a suspected profilin ligand.Keywords
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