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005     20200402210236.0
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|a pmid:22683791
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|a pmc:PMC3370883
024 7 _ |2 DOI
|a 10.1107/S0907444912008372
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082 _ _ |a 570
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|a Biochemical Research Methods
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|a Biochemistry & Molecular Biology
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|a Biophysics
084 _ _ |2 WoS
|a Crystallography
100 1 _ |0 P:(DE-Juel1)131965
|a Granzin, J.
|b 0
|u FZJ
245 _ _ |a Three-dimensional structure of a schistosome serpin revealing an unusual configuration of the helical subdomain
260 _ _ |a Copenhagen
|b Munksgaard
|c 2012
300 _ _ |a 686 - 694
336 7 _ |a Journal Article
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440 _ 0 |0 56
|a Acta Crystallographica D
|v D68
|x 0907-4449
|y 6
500 _ _ |a 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.
520 _ _ |a 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.
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588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Amino Acid Sequence
650 _ 2 |2 MeSH
|a Animals
650 _ 2 |2 MeSH
|a Humans
650 _ 2 |2 MeSH
|a Models, Molecular
650 _ 2 |2 MeSH
|a Molecular Sequence Data
650 _ 2 |2 MeSH
|a Protein Structure, Secondary
650 _ 2 |2 MeSH
|a Protein Structure, Tertiary
650 _ 2 |2 MeSH
|a Schistosoma haematobium: chemistry
650 _ 2 |2 MeSH
|a Sequence Alignment
650 _ 2 |2 MeSH
|a Serpins: chemistry
650 _ 2 |2 MeSH
|a Structural Homology, Protein
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|a Serpins
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700 1 _ |0 P:(DE-HGF)0
|a Huang, Y.
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|a Topbas, C.
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|a Huang, W.
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700 1 _ |0 P:(DE-HGF)0
|a Wu, Z.
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700 1 _ |0 P:(DE-HGF)0
|a Misra, S.
|b 5
700 1 _ |0 P:(DE-HGF)0
|a Hazen, S.L.
|b 6
700 1 _ |0 P:(DE-HGF)0
|a Blanton, R.E.
|b 7
700 1 _ |0 P:(DE-HGF)0
|a Lee, X.
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700 1 _ |0 P:(DE-Juel1)131988
|a Weiergräber, O. H.
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|u FZJ
773 _ _ |0 PERI:(DE-600)2020492-9
|a 10.1107/S0907444912008372
|g Vol. 68, p. 686 - 694
|p 686 - 694
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|t Acta crystallographica / D
|v 68
|x 0907-4449
|y 2012
856 7 _ |2 Pubmed Central
|u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3370883
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