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|Title:||Peptide isomerization induced by pH change regulates the S1 binding site in ficolins||Authors:||Yang, L.
|Issue Date:||2011||Citation:||Yang, L., Zhang, J., Ding, J.L. (2011). Peptide isomerization induced by pH change regulates the S1 binding site in ficolins. Australian Journal of Chemistry 64 (7) : 887-893. ScholarBank@NUS Repository. https://doi.org/10.1071/CH11050||Abstract:||Infection-inflammation mediated interactions between human ficolin and the pathogen GlcNAc is associated with local acidosis, leading to antimicrobial action. Therefore, revealing the precise molecular conformation induced by pH-shift is crucial in understanding the immune response. Here, we performed constant-pH molecular dynamics simulations on the L-ficolin fibrinogen-like domain over pH 4.59. An unusual cis-Asn244-Cys245 peptide bond prevailed over the pH range in the S1 binding site. Analysis of the hydrogen-bond network at S1 suggested Asn244 to be indispensible for maintaining the cis form of Asn244-Cys245, and the absence of the hydroxyl group on Phe262 accounts for the lack of GlcNAc binding. © 2011 CSIRO.||Source Title:||Australian Journal of Chemistry||URI:||http://scholarbank.nus.edu.sg/handle/10635/114370||ISSN:||00049425||DOI:||10.1071/CH11050|
|Appears in Collections:||Staff Publications|
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