Journal Article

PreJuSER-21147

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Three-dimensional structure of a schistosome serpin revealing an unusual configuration of the helical subdomain

Granzin, J.FZJ* ; Huang, Y. ; Topbas, C. ; Huang, W. ; Wu, Z. ; Misra, S. ; Hazen, S. L. ; Blanton, R. E. ; Lee, X. ; Weiergräber, O. H.FZJ*

2012
Munksgaard Copenhagen

This record in other databases:      

Please use a persistent id in citations: doi:10.1107/S0907444912008372

Abstract: 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.

Keyword(s): Amino Acid Sequence (MeSH) ; Animals (MeSH) ; Humans (MeSH) ; Models, Molecular (MeSH) ; Molecular Sequence Data (MeSH) ; Protein Structure, Secondary (MeSH) ; Protein Structure, Tertiary (MeSH) ; Schistosoma haematobium: chemistry (MeSH) ; Sequence Alignment (MeSH) ; Serpins: chemistry (MeSH) ; Structural Homology, Protein (MeSH) ; Serpins ; J

Note: JG and OHW are grateful to Georg Buldt and Dieter Willbold for continuous generous support. XL and SH are supported by NIH grant P01HL076491. Furthermore, excellent assistance by Craig Ogata, the manager of the X4a beamline, and his staff at NSLS is greatly appreciated.

---

Contributing Institute(s):

1. Strukturbiochemie (ICS-6)

Research Program(s):

1. Funktion und Dysfunktion des Nervensystems (P33)
2. BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung (P45)

Appears in the scientific report 2012

---

Database coverage:
; BIOSIS Previews ; Current Contents - Life Sciences ; JCR ; NCBI Molecular Biology Database ; Nationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

---