ArticleBiomolecular NMR assignments2016
(1)H, (15)N, and (13)C resonance assignments of Staphylococcus aureus extracellular adherence protein domain 4.
Article in Biomolecular NMR assignments, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- New advances in understanding inhibition of myeloperoxidase and neutrophil serine proteases by two families of staphylococcal innate immune evasion proteins.Archives of biochemistry and biophysics · 2024Review
- Staphylococcal peroxidase inhibitor (SPIN): Investigation of the inhibitory N-terminal domain via a stabilizing disulfide insertion.Archives of biochemistry and biophysics · 2024Article
- Complete non-proline backbone resonance assignments of the S. aureus neutrophil serine protease inhibitor, EapH1.Biomolecular NMR assignments · 2023Article
- Staphylococcus aureus evasion proteins EapH1 and EapH2: Residue-level investigation of an alternative binding motif for human neutrophil elastase.Archives of biochemistry and biophysics · 2019Article
- Investigation of Human Neutrophil Elastase Inhibition by Staphylococcus aureus EapH1: The Key Role Played by Arginine 89.Biochemistry · 2018Article
- A structurally dynamic N-terminal region drives function of the staphylococcal peroxidase inhibitor (SPIN).The Journal of biological chemistry · 2018Article
- Backbone and side-chainBiomolecular NMR assignments · 2017Article
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5 authors at 1 institution in 1 country.
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Abstract
The pathogenic bacterium Staphylococcus aureus has evolved to actively evade many aspects of the human innate immune system by expressing a series of secreted inhibitory proteins. Among these, the extracellular adherence protein (Eap) has been shown to inhibit the classical and lectin pathways of the complement system. By binding to complement component C4b, Eap is able to inhibit formation of the CP/LP C3 pro-convertase. Secreted full-length, mature Eap consists of four ~98 residue domains, all of which adopt a similar beta-grasp fold, and are connected through a short linker region. Through multiple biochemical approaches, it has been determined that the third and fourth domains of Eap are responsible for C4b binding. Here we report the backbone and side-chain resonance assignments of the 11.3 kDa fourth domain of Eap. The assignment data has been deposited in the BMRB database under the accession number 26726.
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