Citation

BibTex format

@article{Stemberk:2014:10.1074/jbc.M113.543546,
author = {Stemberk, V and Jones, RPO and Moroz, O and Atkin, KE and Edwards, AM and Turkenburg, JP and Leech, AP and Massey, RC and Potts, JR},
doi = {10.1074/jbc.M113.543546},
journal = {Journal of Biological Chemistry},
pages = {12842--12851},
title = {Evidence for steric regulation of fibrinogen binding to staphylococcus aureus Fibronectin-binding Protein A ( FnBPA)},
url = {http://dx.doi.org/10.1074/jbc.M113.543546},
volume = {289},
year = {2014}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - The adjacent fibrinogen (Fg)- and fibronectin (Fn)-binding sites on Fn-binding protein A (FnBPA), a cell surface protein from Staphylococcus aureus, are implicated in the initiation and persistence of infection. FnBPA contains a single Fg-binding site (that also binds elastin) and multiple Fn-binding sites. Here, we solved the structure of the N2N3 domains containing the Fg-binding site of FnBPA in the apo form and in complex with a Fg peptide. The Fg binding mechanism is similar to that of homologous bacterial proteins but without the requirement for “latch” strand residues. We show that the Fg-binding sites and the most N-terminal Fn-binding sites are nonoverlapping but in close proximity. Although Fg and a subdomain of Fn can form a ternary complex on an FnBPA protein construct containing a Fg-binding site and single Fn-binding site, binding of intact Fn appears to inhibit Fg binding, suggesting steric regulation. Given the concentrations of Fn and Fg in the plasma, this mechanism might result in targeting of S. aureus to fibrin-rich thrombi or elastin-rich tissues.
AU  - Stemberk,V
AU  - Jones,RPO
AU  - Moroz,O
AU  - Atkin,KE
AU  - Edwards,AM
AU  - Turkenburg,JP
AU  - Leech,AP
AU  - Massey,RC
AU  - Potts,JR
DO  - 10.1074/jbc.M113.543546
EP  - 12851
PY  - 2014///
SN  - 0021-9258
SP  - 12842
TI  - Evidence for steric regulation of fibrinogen binding to staphylococcus aureus Fibronectin-binding Protein A ( FnBPA)
T2  - Journal of Biological Chemistry
UR  - http://dx.doi.org/10.1074/jbc.M113.543546
UR  - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000335581400053&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR  - https://www.jbc.org/content/289/18/12842
UR  - http://hdl.handle.net/10044/1/83358
VL  - 289
ER  -
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