Lectins on a roll: the structure of E-selectin.
The crystal structure of the lectin/EGF portion of E-selectin confirms anticipated similarities with homologous domains, but reveals some surprising features that emphasize the limitations of homology modelling.
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Department of Cell Biology, Stanford University School of Medicine, CA 94305.
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism; D050260:Carbohydrate Metabolism; D002240:Carbohydrate Sequence; D002352:Carrier Proteins / Q000737:chemistry; D015815:Cell Adhesion Molecules / Q000737:chemistry*; D017124:Conserved Sequence; D019040:E-Selectin; D004815:Epidermal Growth Factor / Q000737:chemistry; D037102:Lectins / Q000737:chemistry* / Q000378:metabolism; D037241:Mannose-Binding Lectins; D008562:Membrane Glycoproteins / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary
D002352:Carrier Proteins; D015815:Cell Adhesion Molecules; D019040:E-Selectin; D037102:Lectins; D037241:Mannose-Binding Lectins; D008562:Membrane Glycoproteins; D004815:Epidermal Growth Factor; D002118:Calcium