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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 ap...

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Main Authors: McGrath, M E, Erpel, T, Bystroff, C, Fletterick, R J
格式: Artigo
語言:Inglês
出版: 1994
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在線閱讀:https://ncbi.nlm.nih.gov/pmc/articles/PMC394978/
https://ncbi.nlm.nih.gov/pubmed/8156987
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