Abstract
The title tetrapeptide, Leu-Arg-Pro-Gly-NH2, forms a complex with trypsin in a novel orthorhombic crystal form with low molecular packing density. The complex formation was directly evidenced by X-ray crystallography. The crystal structure at 1.8 Å resolution was refined to anR-factor of 20.5% for 13,923 reflection data, which were measured with synchrotron radiation. The tetrapeptide is bound to trypsin at the active site, and the binding mode is very similar to that of a bovine pancreatic trypsin inhibitor (BPTI):trypsin complex. The tetrapeptide:trypsin complex is the first observation that a peptide forms a stable complex with trypsin.
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Bartunik, H. D., Summers, L. J., and Bartsch, H. H. (1989).J. Mol. Biol. 210, 813–828.
Bode, W., and Schwager, P. (1975).J. Mol. Biol. 98, 683–692.
Bode, W., Greyling, H. J., Huber, R., Otlewski, J., and Wilusz, T. (1989).FEBS Lett. 242, 285–292.
Chen, Z., and Bode, W. (1983).J. Mol. Biol. 164, 283–311.
Hendrickson, W. A., and Konnert, J. H. (1980). InComputing in Crystallography (Diamond, R., Ramaseshan, S., and Venkatesan, K., eds.), Indian Academy of Sciences, Bangalore, pp. 13.01–13.23.
Higashi, T. (1989).J. Appl. Cryst. 22, 9–18.
Huber, R., Kukla, D., Bode, W., Schwager, P., Bartels, K., Deisenhofer, J., and Steigemann, W. (1974).J. Mol. Biol. 89, 73–101.
Marquart, M., Walter, J., Deisenhofer, J., Bode, W., and Huber, R. (1983).Acta Crystallogr. B39, 480–490.
Matsumoto, O., Taga, T., and Machida, K. (1989).Acta Crystallogr. C45, 913–915.
Matsumoto, O., Taga, T., Matsushima, M., Higashi, T., and Machida, K. (1990).Chem. Pharm. Bull. (in press).
Sakabe, N. (1983).J. Appl. Cryst. 16, 542–547.
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Matsumoto, O., Taga, T., Higashi, T. et al. Complex formation by bovine trypsin and a tetrapeptide (Leu-Arg-Pro-Gly-NH2): X-ray structure analysis of the complex in the orthorhombic crystal form with low molecular packing density. J Protein Chem 9, 589–593 (1990). https://doi.org/10.1007/BF01025012
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DOI: https://doi.org/10.1007/BF01025012