1mtn

From Proteopedia

---

Revision as of 19:34, 20 November 2007

proteopedia linkproteopedia link

spinqualitylabelsall models 1mtn, resolution 2.8Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

BOVINE ALPHA-CHYMOTRYPSIN:BPTI CRYSTALLIZATION

Overview

The crystal structure of bovine alpha-chymotrypsin (alpha-CHT) in complex, with the bovine basic pancreatic trypsin inhibitor (BPTI) has been solved, and refined at 2.8 A resolution (R-factor = 0.18). The, proteinase:inhibitor complex forms a compact dimer (two alpha-CHT and two, BPTI molecules), which may be stabilized by surface-bound sulphate ions, in the crystalline state. Each BPTI molecule, at opposite ends, is, contacting both proteinase molecules in the dimer, through the reactive, site loop and through residues next to the inhibitor's C-terminal region., Specific recognition between alpha-CHT and BPTI occurs at the (re)active, site interface according to structural rules inferred from the analysis of, homologous serine proteinase:inhibitor complexes. Lys15, the P1 residue of, BPTI, however, does not occupy the alpha-CHT S1 specificity pocket, being, hydrogen bonded to backbone atoms of the enzyme surface residues Gly216, and Ser217.

About this Structure

1MTN is a Protein complex structure of sequences from Bos taurus with SO4 as ligand. Active as Chymotrypsin, with EC number 3.4.21.1 Full crystallographic information is available from OCA.

Reference

Crystal structure of the bovine alpha-chymotrypsin:Kunitz inhibitor complex. An example of multiple protein:protein recognition sites., Capasso C, Rizzi M, Menegatti E, Ascenzi P, Bolognesi M, J Mol Recognit. 1997 Jan-Feb;10(1):26-35. PMID:9179777

Page seeded by OCA on Tue Nov 20 21:41:19 2007