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Ensemble refinement shows conformational flexibility in crystal structures of human complement factor D
Human factor D (FD) is a self-inhibited thrombin-like serine proteinase that is critical for amplification of the complement immune response. FD is activated by its substrate through interactions outside the active site. The substrate-binding, or ‘exosite’, region displays a well defined and rigid c...
| Autores principales: | , , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
| Publicado: |
International Union of Crystallography
2014
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3949522/ https://www.ncbi.nlm.nih.gov/pubmed/24598742 http://dx.doi.org/10.1107/S1399004713032549 |