Histidine-Mediated pH-Sensitive Regulation of M-Ficolin:GlcNAc Binding in Innate Immunity Examined by Molecular Dynamics Simulations
Background: M-ficolin, a pathogen recognition molecule in the innate immune system, binds sugar residues including N-acetyl-D-glucosamine (GlcNAc), which is displayed on invading microbes and on apoptotic cells. The cis and trans Asp282-Cys283 peptide bond in the M-ficolin, which was found to occur...
Main Authors: | Yang, Linfeng, Zhang, Jing, Ho, Bow, Ding, Jeak Ling |
---|---|
Other Authors: | Massachusetts Institute of Technology. Computational and Systems Biology Program |
Format: | Article |
Language: | en_US |
Published: |
Public Library of Science
2011
|
Online Access: | http://hdl.handle.net/1721.1/65602 |
Similar Items
-
Natural IgG antibodies provide innate protection against ficolin-opsonized bacteria
by: Panda, Saswati, et al.
Published: (2015) -
A novel human tectonin protein with multivalent beta-propeller folds interacts with ficolin and binds bacterial LPS
by: Low, Dianna Hooi Ping, et al.
Published: (2010) -
GlcNAc-1,6-anhydro-MurNAc moiety affords unusual glycosyl acceptor that terminates peptidoglycan elongation
by: Zhang, Xiao-Lin, et al.
Published: (2024) -
Detecting post-translational modification, O-GlcNAc, on Munc18a protein.
by: Ngow, Yeen Shian.
Published: (2013) -
Biosynthesis of UDP-GlcNAc(3NAc)A by WbpB, WbpE, and WbpD: Enzymes in the Wbp Pathway Responsible for O-antigen Assembly in Pseudomonas aeruginosa PAO1
by: Larkin, Angelyn, et al.
Published: (2012)