Macromolecular chelation as an improved mechanism of protease inhibition: structure of the ecotin-trypsin complex.
The 2.4 A crystal structure (R = 0.180) of the serine protease inhibitor ecotin was determined in a complex with trypsin. Ecotin's dimer structure provides a second discrete and distal binding site for trypsin and, as shown by modelling experiments, other serine proteases. The second site is approxi...
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| Udgivet i: | EMBO J |
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| Principais autores: | , , , |
| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
Nature Publishing Group
1994
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC394978/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8156987/ https://ncbi.nlm.nih.govhttps://doi.org/10.1002/j.1460-2075.1994.tb06411.x |
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