Modelling the carbohydrate recognition domain of human E-selectin.
The three-dimensional structure of the carbohydrate recognition domain of the human E-selectin endothelial-leucocyte adhesion molecule (ELAM-1) was modelled on the basis of the recently determined X-ray crystallographic structure of the homologous domain found in the rat mannose-binding protein. The EGF-like module, which is contiguous to the E-selectin lectin domain, and which is also involved in binding the tetrasaccharide ligand, was modelled on the recently determined NMR structure of the EGF-like module of human factor IX. The rule-based homology modelling procedures developed at Birkbeck and encoded in the program COMPOSER were used. The model of the two domains combined is discussed in terms of cation and ligand binding.
Mills
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Crystallography Department, Birkbeck College, University of London, UK.
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D050260:Carbohydrate Metabolism; D002352:Carrier Proteins / Q000737:chemistry; D015815:Cell Adhesion Molecules / Q000737:chemistry* / Q000378:metabolism; D003198:Computer Simulation; D019040:E-Selectin; D004815:Epidermal Growth Factor / Q000737:chemistry; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D037241:Mannose-Binding Lectins; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D051381:Rats; D017386:Sequence Homology, Amino Acid; D014961:X-Ray Diffraction
D002352:Carrier Proteins; D015815:Cell Adhesion Molecules; D019040:E-Selectin; D037241:Mannose-Binding Lectins; D004815:Epidermal Growth Factor