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Electrostatic interactions of domain III stabilize the inactive conformation of μ-calpain
The ubiquitous μ- and m-calpains are Ca(2+)-dependent cysteine proteases. They are activated via rearrangement of the catalytic domain II induced by cooperative binding of Ca(2+) to several sites of the molecule. Based on the crystallographic structures, a cluster of acidic residues in domain III, t...
Gorde:
| Egile Nagusiak: | , , , , , |
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| Formatua: | Artigo |
| Hizkuntza: | Inglês |
| Argitaratua: |
Portland Press Ltd.
2004
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| Gaiak: | |
| Sarrera elektronikoa: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1133818/ https://ncbi.nlm.nih.gov/pubmed/15180595 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1042/BJ20040731 |
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