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Structural analysis of Efb, a fibrinogen binding protein of Staphylococcus aureus
Karolinska Institutet.ORCID-id: 0000-0002-3049-967X
Vise andre og tillknytning
1998 (engelsk)Inngår i: Protein peptide letters, ISSN 0929-8665, E-ISSN 1875-5305, Vol. 5, nr 4, s. 199-206Artikkel i tidsskrift (Fagfellevurdert) Published
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Text
Abstract [en]

Staphylococcus aureus produces and secretes a small, basic protein, designated Efb, that binds to fibrinogen and seems to be required for virulence of the organism. A 3D model of Efb was developed, and it predicts that the C-terminal half of the protein contains substantial alpha-helical content. CD analysis of Efb yielded a value of 40-41% alpha-helix. Calcium and zinc both influence the interactions between Efb and fibrinogen, and an analysis of the amino acid sequence of Efb revealed the presence of consensus sequences for the binding of both metals.

sted, utgiver, år, opplag, sider
1998. Vol. 5, nr 4, s. 199-206
Emneord [en]
circular-dichroism, coordination, prediction, virulence, zinc
HSV kategori
Identifikatorer
URN: urn:nbn:se:sh:diva-29042ISI: 000075171200003Scopus ID: 2-s2.0-3142565180OAI: oai:DiVA.org:sh-29042DiVA, id: diva2:891578
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Times Cited: 0 Article English Cited References Count: 22 106vm

Tilgjengelig fra: 2016-01-07 Laget: 2016-01-07 Sist oppdatert: 2025-10-07bibliografisk kontrollert

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