Abstract
The solution structure of a synthetic 22‐amino acid peptide (P1) corresponding to the extreme C‐terminal end and one of the F‐actin binding sites of villin has been determined by 1H NMR and CD spectroscopy. The structure of this peptide was compared to that of a peptide in which lysine to glutamic acid substitutions were introduced at positions 17 and 19 (P11), abolishing F‐actin binding. Both peptides are largely unstructured in aqueous solution. Changes observed in the NMR and CD spectra of both peptides are consistent with α‐helix formation in trifluoroethanol/water mixtures. A set of 189 interproton distances derived from nuclear Overhauser enhancement (NOE) measurements, 17 φ‐angle constraints obtained from 3Jnhα coupling constants, as well as about 10 N···O distance restraints deduced from amide proton exchange kinetics with deuterium, were used for the structure determination. The three‐dimensional structure of P1 and P11 is characterized by two helical regions, one extending from residues 2 to 5 and a second covering residues 7 to 17. The central fragment, ranging from Leu‐7 to Leu‐15, is more stable. The C‐terminal residues are less structured, particularly within peptide P11. The significance of these structural results is discussed in relation to the biological activity of villin. © Munksgaard 1995.
Bibliography
SIMENEL, C., ROSE, T., GOETHALS, M., VANDEKERCKHOVE, J., FRIEDERICH, E., LOUVARD, D., & DELEPIERRE, M. (1995). Conformational behaviour of a synthetic peptide of the Câterminus of villin that interacts with actin: an NMR, CD and simulated annealing study. International Journal of Peptide and Protein Research, 45(6), 574â586. Portico.
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Dates
Type | When |
---|---|
Created | 15 years ago (Aug. 9, 2010, 7:52 p.m.) |
Deposited | 1 year, 10 months ago (Oct. 26, 2023, 10:24 p.m.) |
Indexed | 1 year, 7 months ago (Jan. 14, 2024, 2:24 a.m.) |
Issued | 30 years, 3 months ago (June 1, 1995) |
Published | 30 years, 3 months ago (June 1, 1995) |
Published Online | 16 years, 7 months ago (Jan. 12, 2009) |
Published Print | 30 years, 3 months ago (June 1, 1995) |
@article{SIMENEL_1995, title={Conformational behaviour of a synthetic peptide of the C‐terminus of villin that interacts with actin: an NMR, CD and simulated annealing study}, volume={45}, ISSN={0367-8377}, url={http://dx.doi.org/10.1111/j.1399-3011.1995.tb01322.x}, DOI={10.1111/j.1399-3011.1995.tb01322.x}, number={6}, journal={International Journal of Peptide and Protein Research}, publisher={Wiley}, author={SIMENEL, CATHERINE and ROSE, THIERRY and GOETHALS, MARC and VANDEKERCKHOVE, JOËL and FRIEDERICH, EVELYNE and LOUVARD, DANIEL and DELEPIERRE, MURIEL}, year={1995}, month=jun, pages={574–586} }