1f2s
From Proteopedia
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CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN BOVINE BETA-TRYPSIN AND MCTI-A, A TRYPSIN INHIBITOR OF SQUASH FAMILY AT 1.8 A RESOLUTION
Overview
The stoichiometric complex formed between bovine beta-trypsin and, Momordica charantia, Linn. Cucurbitaceae trypsin inhibitor A (MCTI-A) was, crystallized and its X-ray crystal structure was refined to a final R, value of 0.179 using data of 7.0- to 1.8-A resolution. Combination with, results on the complex of MCTI-A with porcine trypsin gives the sequence, of MCTI-A definitely, of which 13 residues are conserved compared with, other squash family trypsin inhibitors. Its spatial structure and the, conformation of its primary binding segment from Cys3I (P3) to Glu7I, (P3'), which contains a reactive scissile bond Arg5I C-Ile6I N, were found, to be very similar to the other squash family proteinase inhibitors.
About this Structure
1F2S is a Protein complex structure of sequences from Bos taurus and Momordica charantia with CA as ligand. This structure superseeds the now removed PDB entry 1MCU. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.
Reference
Crystal structure of the complex formed between bovine beta-trypsin and MCTI-A, a trypsin inhibitor of squash family, at 1.8-A resolution., Zhu Y, Huang Q, Qian M, Jia Y, Tang Y, J Protein Chem. 1999 Jul;18(5):505-9. PMID:10524768
Page seeded by OCA on Tue Nov 20 14:33:25 2007
