| Autor: |
Pedersen DV; Department of Molecular Biology and Genetics, Aarhus University, Gustav Wiedsvej 10C, DK-8000 Aarhus, Denmark., Revel M; Department of Molecular Biology and Genetics, Aarhus University, Gustav Wiedsvej 10C, DK-8000 Aarhus, Denmark., Gadeberg TAF; Department of Molecular Biology and Genetics, Aarhus University, Gustav Wiedsvej 10C, DK-8000 Aarhus, Denmark., Andersen GR; Department of Molecular Biology and Genetics, Aarhus University, Gustav Wiedsvej 10C, DK-8000 Aarhus, Denmark. |
| Jazyk: |
angličtina |
| Zdroj: |
Acta crystallographica. Section F, Structural biology communications [Acta Crystallogr F Struct Biol Commun] 2019 Feb 01; Vol. 75 (Pt 2), pp. 0. Date of Electronic Publication: 2019 Jan 23. |
| DOI: |
10.1107/S2053230X18018150 |
| Abstrakt: |
The 54 kDa protein properdin, also known as factor P (FP), plays a major role in the complement system through the stabilization of the alternative pathway convertases. FP circulates in the blood as cyclic dimers, trimers and tetramers, and this heterogeneity challenges detailed structural insight into the mechanism of convertase stabilization by FP. Here, the generation of an intact FP monomer and a variant monomer with the third thrombospondin repeat liberated is described. Both FP monomers were excised from recombinant full-length FP containing internal cleavage sites for TEV protease. These FP monomers could be crystallized, and complete data sets extending to 2.8 Å resolution for the intact FP monomer and to 3.5 Å resolution for the truncated variant were collected. The principle of specific monomer excision and domain removal by the insertion of a protease cleavage site may be broadly applicable to structural studies of oligomeric, flexible and modular proteins. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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