Increasing diversity of animal lectin structures.
The number of animal proteins known to recognize carbohydrates and the number of their biological roles continue to increase. Comparisons of primary structures show that some of the newly described lectins are akin to previously investigated lectins, whereas others represent new structural groups. Progress has been made in understanding structure-function relationships for several lectins in both the old and the new categories.
Drickamer
K
K
Department of Biochemistry, University of Oxford, UK.
D000818:Animals; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism; D015815:Cell Adhesion Molecules / Q000737:chemistry / Q000378:metabolism; D006388:Hemagglutinins / Q000737:chemistry / Q000378:metabolism; D007136:Immunoglobulins / Q000737:chemistry / Q000378:metabolism; D037102:Lectins / Q000737:chemistry* / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000737:chemistry / Q000378:metabolism; D011971:Receptors, Immunologic / Q000737:chemistry / Q000378:metabolism; D063267:Sialic Acid Binding Ig-like Lectin 1
D015815:Cell Adhesion Molecules; D006388:Hemagglutinins; D007136:Immunoglobulins; D037102:Lectins; D008562:Membrane Glycoproteins; D011971:Receptors, Immunologic; D063267:Sialic Acid Binding Ig-like Lectin 1; D002118:Calcium