Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Lewis X trisaccharides normally function as essential cell-cell interaction mediators. However, oligomers of Lewis X trisaccharides expressed by the parasite Schistosoma mansoni seem to be related to its evasion of the immune response of its human host. Here we show that monoclonal antibody 54-5C10-A, which is used to diagnose schistosomiasis in humans, interacts with oligomers of at least three Lewis X trisaccharides, but not with monomeric Lewis X. We describe the sequence and the 2.5 A crystal structure of its Fab fragment and infer a possible mode of binding of the polymeric Lewis X from docking studies. Our studies indicate a radically different mode of binding compared to Fab 291-2G3-A, which is specific for monomeric Lewis X, thus providing a structural explanation of the diagnostic success of 54-5C10-A.
Characterization of a diagnostic Fab fragment binding trimeric Lewis X.,de Geus DC, van Roon AM, Thomassen EA, Hokke CH, Deelder AM, Abrahams JP Proteins. 2009 Aug 1;76(2):439-47. PMID:19173313[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ de Geus DC, van Roon AM, Thomassen EA, Hokke CH, Deelder AM, Abrahams JP. Characterization of a diagnostic Fab fragment binding trimeric Lewis X. Proteins. 2009 Aug 1;76(2):439-47. PMID:19173313 doi:10.1002/prot.22356
