This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1ab9
From Proteopedia
|
CRYSTAL STRUCTURE OF BOVINE GAMMA-CHYMOTRYPSIN
Overview
The dipeptide D-leucyl-L-phenylalanyl p-fluorobenzylamide, (D-Leu-Phe-NH-BzlF) inhibits chymotrypsin strongly in a competitive manner, with the Ki value of 0.61 microM [Shimohigashi, Y., Maeda, I., Nose, T., Ikesue, K., Sakamoto, H., Ogawa, T., Ide, Y., Kawahara, M., Nezu, T., Terada, Y., Kawano, K. & Ohno, M. (1996) J. Chem. Soc. Perkin Trans. 1, 2479-2485]. The structure/activity studies have suggested a unique, inhibitory conformation, in which the C-terminal benzyl group fits the, chymotrypsin S1 site and the hydrophobic core constructed by the side, chains of D-Leu-Phe fits the S2 or S1' site. To verify this assumption, the molecular structure of the complex between the dipeptide and, gamma-chymotrypsin has been determined crystallographically., Gamma-chymotrypsin itself was ... [(full description)]
About this Structure
1AB9 is a [Protein complex] structure of sequences from [Bos taurus] with SO4 as [ligand]. Active as [Chymotrypsin], with EC number [3.4.21.1]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].
Reference
X-ray crystal structure of a dipeptide-chymotrypsin complex in an inhibitory interaction., Kashima A, Inoue Y, Sugio S, Maeda I, Nose T, Shimohigashi Y, Eur J Biochem. 1998 Jul 1;255(1):12-23. PMID:9692896
Page seeded by OCA on Tue Oct 30 14:46:46 2007
