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Crystal structure analyses of uncomplexed ecotin in two crystal forms: implications for its function and stability.
Ecotin, a homodimeric protein composed of 142 residue subunits, is a novel serine protease inhibitor present in Escherichia coli. Its thermostability and acid stability, as well as broad specificity toward proteases, make it an interesting protein for structural characterization. Its structure in th...
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| Hlavní autoři: | , , , , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
Cold Spring Harbor Laboratory Press
1996
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2143284/ https://ncbi.nlm.nih.gov/pubmed/8931142 |
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