1mct
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THE REFINED 1.6 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN PORCINE BETA-TRYPSIN AND MCTI-A, A TRYPSIN INHIBITOR OF SQUASH FAMILY
OverviewOverview
The crystal structure of the complex formed by porcine beta-trypsin with, the MCTI-A inhibitor (Momordica charantia, Linn. Cucurbitaceae) has been, determined at 1.6 A resolution using the molecular replacement method. The, sequence of MCTI-A was determined by recognizing the electron density, and, shows that MCTI-A is a member of the squash family of trypsin inhibitors., We report the first high-resolution structure of porcine beta-trypsin., Detailed comparisons have been made on the overall structure, solvent, structure and active-site geometries between this complex and bovine, beta-trypsin and its complexes. On the basis of our results, we discuss, the interaction patterns between inhibitor and trypsin. Unlike other, complex structures formed by bovine trypsin with inhibitors, no, out-of-plane distortion around the inhibitor's scissible peptide was, observed. The role of the trypsin catalytic triad is also discussed on the, basis of this structure.
About this StructureAbout this Structure
1MCT is a Protein complex structure of sequences from Momordica charantia and Sus scrofa with CA as ligand. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.
ReferenceReference
Refined 1.6 A resolution crystal structure of the complex formed between porcine beta-trypsin and MCTI-A, a trypsin inhibitor of the squash family. Detailed comparison with bovine beta-trypsin and its complex., Huang Q, Liu S, Tang Y, J Mol Biol. 1993 Feb 20;229(4):1022-36. PMID:8445634
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