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.
journal_name
Biomol NMR Assignjournal_title
Biomolecular NMR assignmentsauthors
Woehl JL,Takahashi D,Herrera AI,Geisbrecht BV,Prakash Odoi
10.1007/s12104-016-9688-5subject
Has Abstractpub_date
2016-10-01 00:00:00pages
301-5issue
2eissn
1874-2718issn
1874-270Xpii
10.1007/s12104-016-9688-5journal_volume
10pub_type
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