Molecular modelling of MHC class I carbohydrates.
In this article we present the results of molecular modelling of four complex carbohydrates which have been found in the MHC class I proteins. Though these proteins show diversity in their sequences, the glycosylation sites are highly conserved indicating a possible structural/functional role of the glycan chain. Similar glycan chains have been found linked with other proteins of completely different function, such as IgG, and erythropoeitin. Thus, the molecular modelling of these carbohydrates will not only provide structural/dynamic information of these complex molecules but will also provide conformational information which can be utilised to build the glycoprotein models. The results presented here indicate that although several linkages show less conformational flexibility, terminal linkages can be quite flexible.
Mandal
T K
TK
Department of Chemistry, University of Calcutta, 92, APC. Road, Calcutta 700 009, India.
Mukhopadhyay
C
C
D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D002241:Carbohydrates / Q000737:chemistry*; D004187:Disaccharides / Q000737:chemistry; D004921:Erythropoietin / Q000737:chemistry; D007074:Immunoglobulin G / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D008285:Major Histocompatibility Complex; D008958:Models, Molecular; D008969:Molecular Sequence Data; D012984:Software; D013050:Spectrometry, Fluorescence; D013997:Time Factors
D002241:Carbohydrates; D004187:Disaccharides; D007074:Immunoglobulin G; D004921:Erythropoietin