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000144054 0247_ $$2pmid$$apmid:22579681
000144054 0247_ $$2doi$$a10.1016/j.jsb.2012.04.023
000144054 0247_ $$2ISSN$$a1047-8477
000144054 0247_ $$2ISSN$$a1095-8657
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000144054 037__ $$aPHPPUBDB-25783
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000144054 1001_ $$aBoix, E.
000144054 1101_ $$aDESY$$bExperiments with synchrotron radiation
000144054 245__ $$aThe sulfate-binding site structure of the human eosinophil cationic protein as revealed by a new crystal form
000144054 260__ $$aSan Diego, Calif.$$bElsevier$$c2012
000144054 300__ $$a1-9
000144054 3367_ $$00$$2EndNote$$aJournal Article
000144054 3367_ $$2BibTeX$$aARTICLE
000144054 3367_ $$2DRIVER$$aarticle
000144054 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$mjournal
000144054 440_0 $$0PERI:(DE-600)1469822-5$$aJ. Struct. Biol.$$v179(1)$$x1047-8477
000144054 500__ $$3Converted on 2013-05-30 10:00
000144054 500__ $$3Converted on 2013-06-21 19:21
000144054 520__ $$aThe human eosinophil cationic protein (ECP), also known as RNase 3, is an eosinophil secretion protein that is involved in innate immunity and displays antipathogen and proinflammatory activities. ECP has a high binding affinity for heterosaccharides, such as bacterial lipopolysaccharides and heparan sulfate found in the glycocalix of eukaryotic cells. We have crystallized ECP in complex with sulfate anions in a new monoclinic crystal form. In this form, the active site groove is exposed, providing an alternative model for ligand binding studies. By exploring the protein-sulfate complex, we have defined the sulfate binding site architecture. Three main sites (S1-S3) are located in the protein active site; S1 and S2 overlap with the phosphate binding sites involved in RNase nucleotide recognition. A new site (S3) that is unique to ECP is one of the key anchoring points for sulfated ligands. Arg 1 and Arg 7 in S3, together with Arg 34 and Arg 36 in S1, form the main basic clusters that assist in the recognition of ligand anionic groups. The location of additional sulfate bound molecules, some of which contribute to the crystal packing, may mimic the binding to extended anionic polymers. In conclusion, the structural data define a binding pattern for the recognition of sulfated molecules that can modulate the role of ECP in innate immunity. The results reveal the structural basis for the high affinity of ECP for glycosaminoglycans and can assist in structure-based drug design of inhibitors of the protein cytotoxicity to host tissues during inflammation.
000144054 536__ $$0G:(DE-H253)POF2-K1.1-20130405$$aDORIS Beamline K1.1 (POF2-54G13)$$cPOF2-54G13$$fPOF II$$x0
000144054 588__ $$aDataset connected to Pubmed
000144054 650_2 $$2MeSH$$aAmino Acid Sequence
000144054 650_2 $$2MeSH$$aCatalytic Domain
000144054 650_2 $$2MeSH$$aCrystallization
000144054 650_2 $$2MeSH$$aEosinophil Cationic Protein: chemistry
000144054 650_2 $$2MeSH$$aEosinophil Cationic Protein: metabolism
000144054 650_2 $$2MeSH$$aGlycosaminoglycans: chemistry
000144054 650_2 $$2MeSH$$aGlycosaminoglycans: metabolism
000144054 650_2 $$2MeSH$$aHumans
000144054 650_2 $$2MeSH$$aLigands
000144054 650_2 $$2MeSH$$aMolecular Dynamics Simulation
000144054 650_2 $$2MeSH$$aMolecular Sequence Data
000144054 650_2 $$2MeSH$$aProtein Binding
000144054 650_2 $$2MeSH$$aProtein Conformation
000144054 650_2 $$2MeSH$$aRecombinant Proteins: chemistry
000144054 650_2 $$2MeSH$$aRecombinant Proteins: metabolism
000144054 650_2 $$2MeSH$$aSulfates: chemistry
000144054 650_7 $$00$$2NLM Chemicals$$aGlycosaminoglycans
000144054 650_7 $$00$$2NLM Chemicals$$aLigands
000144054 650_7 $$00$$2NLM Chemicals$$aRecombinant Proteins
000144054 650_7 $$00$$2NLM Chemicals$$aSulfates
000144054 650_7 $$0EC 3.1.27.-$$2NLM Chemicals$$aEosinophil Cationic Protein
000144054 693__ $$0EXP:(DE-H253)D-K1.1-20150101$$1EXP:(DE-H253)DORISIII-20150101$$6EXP:(DE-H253)D-K1.1-20150101$$aDORIS III$$fDORIS Beamline K1.1$$x0
000144054 7001_ $$aPulido, D.
000144054 7001_ $$aMoussaoui, M.
000144054 7001_ $$aNogues, M. V.
000144054 7001_ $$aRussi, S.
000144054 773__ $$0PERI:(DE-600)1469822-5$$a10.1016/j.jsb.2012.04.023$$gVol. 179, p. 1-9$$p1-9$$q179<1-9$$tJournal of structural biology$$v179$$x1047-8477$$y2012
000144054 909CO $$ooai:bib-pubdb1.desy.de:144054$$pVDB
000144054 9101_ $$0I:(DE-HGF)0$$aExternes Institut$$kExtern
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000144054 9141_ $$y2012
000144054 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
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000144054 915__ $$0StatID:(DE-HGF)1$$2StatID$$aNo Author Disambiguation
000144054 920_1 $$iExperiments with synchrotron radiation$$kHASYLAB
000144054 9201_ $$0I:(DE-H253)HASYLAB_-2012_-20130307$$kHASYLAB$$lExperiments with synchrotron radiation$$x0
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000144054 980__ $$aConvertedRecord