Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhu Y, Huang Q, Chi C. Crystal structure of mung bean inhibitor lysine active fragment complex with bovine beta-trypsin at 1.8A resolution. J Biomol Struct Dyn. 1999 Jun;16(6):1219-24. PMID:10447205
