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...

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Detalles Bibliográficos
Autores principales: Forneris, Federico, Burnley, B. Tom, Gros, Piet
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2014
Materias:
Research Papers
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

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3949522/
https://www.ncbi.nlm.nih.gov/pubmed/24598742
http://dx.doi.org/10.1107/S1399004713032549

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