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000055020 084__ $$2WoS$$aMedicine, Research & Experimental
000055020 1001_ $$0P:(DE-Juel1)VDB65446$$aHaenel, K.$$b0$$uFZJ
000055020 245__ $$aSolution structure of the X4 protein coded by the SARS related coronavirus reveals an immunoglobulin like fold and suggests a binding activity to integrin I domains
000055020 260__ $$aLondon$$bBioMed Central$$c2006
000055020 300__ $$a281 - 293
000055020 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000055020 440_0 $$014721$$aJournal of Biomedical Science$$v13$$x1021-7770
000055020 500__ $$aRecord converted from VDB: 12.11.2012
000055020 520__ $$aThe SARS related Coronavirus genome contains a variety of novel accessory genes. One of these, called ORF7a or ORF8, code for a protein, known as 7a, U122 or X4. We set out to determine the three-dimensional structure of the soluble ectodomain of this type-I transmembrane protein by nuclear magnetic resonance spectroscopy. The fold of the protein is the first member of a further variation of the immunoglobulin like beta-sandwich fold. Because X4 does not reveal significant sequence homologies to proteins in the data bases, we carried out a structure based similarity search for proteins with known function. High structural similarity to Dl domains of ICAM-1 and ICAM-2, and common features in amino acid sequence between X4 and ICAM-1, suggest X4 to possess binding activity for the alpha(L) integrin I domain of LFA-1. Further, based on this structure based prediction, potential functions of X4 in virus replication and pathogenesis are discussed.
000055020 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000055020 588__ $$aDataset connected to Web of Science, Pubmed
000055020 650_2 $$2MeSH$$aAmino Acid Sequence
000055020 650_2 $$2MeSH$$aAntigens, CD: chemistry
000055020 650_2 $$2MeSH$$aCell Adhesion Molecules: chemistry
000055020 650_2 $$2MeSH$$aCloning, Molecular
000055020 650_2 $$2MeSH$$aHumans
000055020 650_2 $$2MeSH$$aImmunoglobulins: chemistry
000055020 650_2 $$2MeSH$$aIntegrins: chemistry
000055020 650_2 $$2MeSH$$aIntercellular Adhesion Molecule-1: chemistry
000055020 650_2 $$2MeSH$$aInterleukin-1: chemistry
000055020 650_2 $$2MeSH$$aLymphocyte Function-Associated Antigen-1: chemistry
000055020 650_2 $$2MeSH$$aModels, Molecular
000055020 650_2 $$2MeSH$$aMolecular Sequence Data
000055020 650_2 $$2MeSH$$aOpen Reading Frames
000055020 650_2 $$2MeSH$$aProtein Structure, Secondary
000055020 650_2 $$2MeSH$$aProtein Structure, Tertiary
000055020 650_2 $$2MeSH$$aSARS Virus: chemistry
000055020 650_2 $$2MeSH$$aViral Matrix Proteins: chemistry
000055020 650_2 $$2MeSH$$aViral Proteins: chemistry
000055020 650_7 $$00$$2NLM Chemicals$$aAntigens, CD
000055020 650_7 $$00$$2NLM Chemicals$$aCell Adhesion Molecules
000055020 650_7 $$00$$2NLM Chemicals$$aImmunoglobulins
000055020 650_7 $$00$$2NLM Chemicals$$aIntegrins
000055020 650_7 $$00$$2NLM Chemicals$$aInterleukin-1
000055020 650_7 $$00$$2NLM Chemicals$$aLymphocyte Function-Associated Antigen-1
000055020 650_7 $$00$$2NLM Chemicals$$aViral Matrix Proteins
000055020 650_7 $$00$$2NLM Chemicals$$aViral Proteins
000055020 650_7 $$00$$2NLM Chemicals$$asars7a protein, SARS virus
000055020 650_7 $$0126547-89-5$$2NLM Chemicals$$aIntercellular Adhesion Molecule-1
000055020 650_7 $$0NM_000873$$2NLM Chemicals$$aICAM2 protein, human
000055020 650_7 $$2WoSType$$aJ
000055020 65320 $$2Author$$a7a
000055020 65320 $$2Author$$acoronavirus
000055020 65320 $$2Author$$aimmunoglobulin fold
000055020 65320 $$2Author$$aintegrin
000055020 65320 $$2Author$$aLFA-1
000055020 65320 $$2Author$$aNMR structure determination
000055020 65320 $$2Author$$aORF8
000055020 65320 $$2Author$$aSARS
000055020 65320 $$2Author$$aU122
000055020 65320 $$2Author$$aX4
000055020 7001_ $$0P:(DE-Juel1)VDB8627$$aStangler, T.$$b1$$uFZJ
000055020 7001_ $$0P:(DE-Juel1)VDB21601$$aStoldt, M.$$b2$$uFZJ
000055020 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b3$$uFZJ
000055020 773__ $$0PERI:(DE-600)1482918-6$$a10.1007/s11373-005-9043-9$$gVol. 13, p. 281 - 293$$p281 - 293$$q13<281 - 293$$tJournal of biomedical science$$v13$$x1021-7770$$y2006
000055020 8567_ $$uhttp://dx.doi.org/10.1007/s11373-005-9043-9
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