抄録
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.
| 元の言語 | 英語 |
|---|---|
| ページ（範囲） | 301-305 |
| ページ数 | 5 |
| ジャーナル | Biomolecular NMR Assignments |
| 巻 | 10 |
| 発行部数 | 2 |
| DOI | |
| 出版物ステータス | 出版済み - 10 1 2016 |
| 外部発表 | Yes |
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All Science Journal Classification (ASJC) codes
- Structural Biology
- Biochemistry
これを引用
1H, 15N, and 13C resonance assignments of Staphylococcus aureus extracellular adherence protein domain 4. / Woehl, Jordan L.; Takahashi, Daisuke; Herrera, Alvaro I.; Geisbrecht, Brian V.; Prakash, Om.
：: Biomolecular NMR Assignments, 巻 10, 番号 2, 01.10.2016, p. 301-305.研究成果: ジャーナルへの寄稿 › 記事
}
TY - JOUR
T1 - 1H, 15N, and 13C resonance assignments of Staphylococcus aureus extracellular adherence protein domain 4
AU - Woehl, Jordan L.
AU - Takahashi, Daisuke
AU - Herrera, Alvaro I.
AU - Geisbrecht, Brian V.
AU - Prakash, Om
PY - 2016/10/1
Y1 - 2016/10/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84976480595&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84976480595&partnerID=8YFLogxK
U2 - 10.1007/s12104-016-9688-5
DO - 10.1007/s12104-016-9688-5
M3 - Article
C2 - 27372920
AN - SCOPUS:84976480595
VL - 10
SP - 301
EP - 305
JO - Biomolecular NMR Assignments
JF - Biomolecular NMR Assignments
SN - 1874-2718
IS - 2
ER -