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000021147 084__ $$2WoS$$aBiochemical Research Methods
000021147 084__ $$2WoS$$aBiochemistry & Molecular Biology
000021147 084__ $$2WoS$$aBiophysics
000021147 084__ $$2WoS$$aCrystallography
000021147 1001_ $$0P:(DE-Juel1)131965$$aGranzin, J.$$b0$$uFZJ
000021147 245__ $$aThree-dimensional structure of a schistosome serpin revealing an unusual configuration of the helical subdomain
000021147 260__ $$aCopenhagen$$bMunksgaard$$c2012
000021147 300__ $$a686 - 694
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000021147 440_0 $$056$$aActa Crystallographica D$$vD68$$x0907-4449$$y6
000021147 500__ $$aJG and OHW are grateful to Georg Buldt and Dieter Willbold for continuous generous support. XL and SH are supported by NIH grant P01HL076491. Furthermore, excellent assistance by Craig Ogata, the manager of the X4a beamline, and his staff at NSLS is greatly appreciated.
000021147 520__ $$aParasitic 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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000021147 650_2 $$2MeSH$$aAmino Acid Sequence
000021147 650_2 $$2MeSH$$aAnimals
000021147 650_2 $$2MeSH$$aHumans
000021147 650_2 $$2MeSH$$aModels, Molecular
000021147 650_2 $$2MeSH$$aMolecular Sequence Data
000021147 650_2 $$2MeSH$$aProtein Structure, Secondary
000021147 650_2 $$2MeSH$$aProtein Structure, Tertiary
000021147 650_2 $$2MeSH$$aSchistosoma haematobium: chemistry
000021147 650_2 $$2MeSH$$aSequence Alignment
000021147 650_2 $$2MeSH$$aSerpins: chemistry
000021147 650_2 $$2MeSH$$aStructural Homology, Protein
000021147 650_7 $$00$$2NLM Chemicals$$aSerpins
000021147 650_7 $$2WoSType$$aJ
000021147 7001_ $$0P:(DE-HGF)0$$aHuang, Y.$$b1
000021147 7001_ $$0P:(DE-HGF)0$$aTopbas, C.$$b2
000021147 7001_ $$0P:(DE-HGF)0$$aHuang, W.$$b3
000021147 7001_ $$0P:(DE-HGF)0$$aWu, Z.$$b4
000021147 7001_ $$0P:(DE-HGF)0$$aMisra, S.$$b5
000021147 7001_ $$0P:(DE-HGF)0$$aHazen, S.L.$$b6
000021147 7001_ $$0P:(DE-HGF)0$$aBlanton, R.E.$$b7
000021147 7001_ $$0P:(DE-HGF)0$$aLee, X.$$b8
000021147 7001_ $$0P:(DE-Juel1)131988$$aWeiergräber, O. H.$$b9$$uFZJ
000021147 773__ $$0PERI:(DE-600)2020492-9$$a10.1107/S0907444912008372$$gVol. 68, p. 686 - 694$$p686 - 694$$q68<686 - 694$$tActa crystallographica / D$$v68$$x0907-4449$$y2012
000021147 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3370883
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