1sbw
From Proteopedia
CRYSTAL STRUCTURE OF MUNG BEAN INHIBITOR LYSINE ACTIVE FRAGMENT COMPLEX WITH BOVINE BETA-TRYPSIN AT 1.8A RESOLUTION
Overview
The crystal structure of the complex of mung bean inhibitor lysine active fragment with bovine beta-trypsin has been determined by X-ray crystallographic analysis at a resolution of 1.8 A. Refinement of the model of the complex converged at a final R value of 0.16. From the resulting electron density map, about one-third of the residues of the inhibitor were identified and two residues, at position P4 and P2' respectively, were found to be inconsistent with the sequence reported previously. The peptide chain of the inhibitor at the trypsin active site turns back sharply at Pro23I and forms a 9-residue reactive loop, which interacts with trypsin in a similar manner to the other families of inhibitors, suggesting an important and common role of these regions in exhibiting inhibitory activity.
About this Structure
1SBW is a Protein complex structure of sequences from Bos taurus and Vigna radiata. Full crystallographic information is available from OCA.
Reference
Crystal structure of mung bean inhibitor lysine active fragment complex with bovine beta-trypsin at 1.8A resolution., Zhu Y, Huang Q, Chi C, J Biomol Struct Dyn. 1999 Jun;16(6):1219-24. PMID:10447205 Page seeded by OCA on Sat May 3 08:31:33 2008
Categories: Bos taurus | Protein complex | Trypsin | Vigna radiata | Chi, C. | Huang, Q. | Tang, Y. | Zhu, Y.
