This title appears in the Scientific Report :
2012
Please use the identifier:
http://dx.doi.org/10.1107/S0907444912008372 in citations.
Three-dimensional structure of a schistosome serpin revealing an unusual configuration of the helical subdomain
Three-dimensional structure of a schistosome serpin revealing an unusual configuration of the helical subdomain
Parasitic organisms are constantly challenged by the defence mechanisms of their respective hosts, which often depend on serine protease activities. Consequently, protease inhibitors such as those belonging to the serpin superfamily have emerged as protective elements that support the survival of th...
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Personal Name(s): | Granzin, J. |
---|---|
Huang, Y. / Topbas, C. / Huang, W. / Wu, Z. / Misra, S. / Hazen, S.L. / Blanton, R.E. / Lee, X. / Weiergräber, O. H. | |
Contributing Institute: |
Strukturbiochemie; ICS-6 |
Published in: | Acta crystallographica / D, 68 (2012) S. 686 - 694 |
Imprint: |
Copenhagen
Munksgaard
2012
|
Physical Description: |
686 - 694 |
PubMed ID: |
22683791 |
DOI: |
10.1107/S0907444912008372 |
Document Type: |
Journal Article |
Research Program: |
BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung Funktion und Dysfunktion des Nervensystems |
Series Title: |
Acta Crystallographica D
D68 |
Subject (ZB): | |
Publikationsportal JuSER |
Parasitic organisms are constantly challenged by the defence mechanisms of their respective hosts, which often depend on serine protease activities. Consequently, protease inhibitors such as those belonging to the serpin superfamily have emerged as protective elements that support the survival of the parasites. This report describes the crystal structure of ShSPI, a serpin from the trematode Schistosoma haematobium. The protein is exposed on the surface of invading cercaria as well as of adult worms, suggesting its involvement in the parasite-host interaction. While generally conforming to the well established serpin fold, the structure reveals several distinctive features, mostly concerning the helical subdomain of the protein. It is proposed that these peculiarities are related to the unique biological properties of a small serpin subfamily which is conserved among pathogenic schistosomes. |