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10.1042/BCJ20170085 http://scihub22266oqcxt.onion/10.1042/BCJ20170085 C5415847!5415847!28258151     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28258151&cmd=llinks): Failed to open stream: HTTP request failed! 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Staphylococcus aureus SdrE captures complement factor H s C-terminus via a novel ?close, dock, lock and latch mechanism for complement evasion |pdf=|usr=}}{{28258151}} gab.com Text Staphylococcus aureus SdrE captures complement factor H s C-terminus via a novel close, dock, lock and latch mechanism for complement evasion JO: Biochem J http://www.kidney.de/pget.php?&tw=1&pmid=28258151 #FOAvip Complement factor H (CFH) is a soluble complement regulatory protein essential for the down-regulation of the alternative pathway on interaction with specific markers on the host cell surface. It recognizes the complement component 3b (C3b) and 3d (C3d) fragments in addition to self cell markers (i.e. glycosaminoglycans, sialic acid) to distinguish host cells that deserve protection from pathogens that should be eliminated. The Staphylococcus aureus surface protein serine?aspartate repeat protein E (SdrE) was previously reported to bind human CFH as an immune-evasion tactic. However, the molecular mechanism underlying SdrE?CFH-mediated immune evasion remains unknown. In the present study, we identified a novel region at CFH's C-terminus (CFH1206?1226), which binds SdrE N2 and N3 domains (SdrEN2N3) with high affinity, and determined the crystal structures of apo-SdrEN2N3 and the SdrEN2N3?CFH1206?1226 complex. Comparison of the structure of the CFH?SdrE complex with other CFH structures reveals that CFH's C-terminal tail flips from the main body to insert into the ligand-binding groove of SdrE. In addition, SdrEN2N3 adopts a ?close? state in the absence of CFH, which undergoes a large conformational change on CFH binding, suggesting a novel ?close, dock, lock and latch' (CDLL) mechanism for SdrE to recognize its ligand. Our findings imply that SdrE functions as a ?clamp' to capture CFH's C-terminal tail via a unique CDLL mechanism and sequesters CFH on the surface of S. aureus for complement evasion. Twit Text FOAVip Staphylococcus aureus SdrE captures complement factor H s C-terminus via a novel close, dock, lock and latch mechanism for complement evasion ????Biochem J http://www.kidney.de/pget.php?&tw=1&pmid=28258151 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28258151 #FOAvip English Wikipedia <ref>{{Cite pmid|28258151}}</ref> Staphylococcus aureus SdrE captures complement factor H s C-terminus via a novel ?close, dock, lock and latch mechanism for complement evasion #MMPMID28258151 Zhang Y; Wu M; Hang T; Wang C; Yang Y; Pan W; Zang J; Zhang M; Zhang X Biochem J 2017[May]; 474 (10): 1619-31 PMID28258151show ga Complement factor H (CFH) is a soluble complement regulatory protein essential for the down-regulation of the alternative pathway on interaction with specific markers on the host cell surface. It recognizes the complement component 3b (C3b) and 3d (C3d) fragments in addition to self cell markers (i.e. glycosaminoglycans, sialic acid) to distinguish host cells that deserve protection from pathogens that should be eliminated. The Staphylococcus aureus surface protein serine?aspartate repeat protein E (SdrE) was previously reported to bind human CFH as an immune-evasion tactic. However, the molecular mechanism underlying SdrE?CFH-mediated immune evasion remains unknown. In the present study, we identified a novel region at CFH's C-terminus (CFH1206?1226), which binds SdrE N2 and N3 domains (SdrEN2N3) with high affinity, and determined the crystal structures of apo-SdrEN2N3 and the SdrEN2N3?CFH1206?1226 complex. Comparison of the structure of the CFH?SdrE complex with other CFH structures reveals that CFH's C-terminal tail flips from the main body to insert into the ligand-binding groove of SdrE. In addition, SdrEN2N3 adopts a ?close? state in the absence of CFH, which undergoes a large conformational change on CFH binding, suggesting a novel ?close, dock, lock and latch' (CDLL) mechanism for SdrE to recognize its ligand. Our findings imply that SdrE functions as a ?clamp' to capture CFH's C-terminal tail via a unique CDLL mechanism and sequesters CFH on the surface of S. aureus for complement evasion. �Staphylococcus aureus SdrE captures complement factor H s C-terminus v(epmc).pdf DeepDyve Pubget Overpricing