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Extensive contacts between ADAMTS13 exosites and von Willebrand factor domain A2 contribute to substrate specificity
The metalloprotease ADAMTS13 efficiently cleaves only the Tyr(1605)-Met(1606) bond in the central A2 domain of multimeric von Willebrand factor (VWF), even though VWF constitutes only 0.02% of plasma proteins. This remarkable specificity depends in part on binding of the noncatalytic ADAMTS13 spacer...
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| Главные авторы: | , , |
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| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
American Society of Hematology
2008
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| Предметы: | |
| Online-ссылка: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2518881/ https://ncbi.nlm.nih.gov/pubmed/18492952 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1182/blood-2008-04-148759 |
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