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
