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Structural basis of profactor D activation: from a highly flexible zymogen to a novel self-inhibited serine protease, complement factor D.
The crystal structure of profactor D, determined at 2.1 A resolution with an Rfree and an R-factor of 25.1 and 20.4%, respectively, displays highly flexible or disordered conformation for five regions: N-22, 71-76, 143-152, 187-193 and 215-223. A comparison with the structure of its mature serine pr...
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| Main Authors: | , , , , , |
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| Format: | Artigo |
| Jezik: | Inglês |
| Izdano: |
1999
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| Teme: | |
| Online dostop: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1171173/ https://ncbi.nlm.nih.gov/pubmed/10022823 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/emboj/18.4.804 |
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