I-type lectins

• Published in: BBA - General Subjects Vol. 1572; no. 2; pp. 294 - 316
• Main Authors: Angata, Takashi, Brinkman-Van der Linden, Els C.M
• Format: Book Review Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 19.09.2002
• Subjects: Animals; Antigens, CD - chemistry; Antigens, CD - metabolism; Cell adhesion molecule; Glycoconjugates - chemistry; Glycoconjugates - metabolism; Glycosaminoglycans - chemistry; Glycosaminoglycans - metabolism; Humans; I-type lectin; Immunoglobulins - metabolism; Lectin; Lectins - classification; Lectins - metabolism; Membrane Glycoproteins - chemistry; Membrane Glycoproteins - metabolism; N-Acetylneuraminic Acid - metabolism; Protein Structure, Tertiary; Receptors, Immunologic - chemistry; Receptors, Immunologic - metabolism; Sialic Acid Binding Ig-like Lectin 1; Siglec; Lectin; GPI; Siglec; NCAM; FGF(R); Neu5Ac; Cell adhesion molecule; IgIV; GAG; Neu5Gc; ITIM; OB-BP1; MAG; CRD; ITAM; I-type lectin; SMP; AIRM1; EBV; FISH; Sn; NK; Ig; FNIII
• ISSN: 0304-4165; 0006-3002; 1872-8006
• DOI: 10.1016/S0304-4165(02)00316-1

The immunoglobulin superfamily is a large category of proteins defined by their structural similarity to immunoglobulins. The majority of these proteins are involved in protein–protein binding as receptors, antibodies or cell adhesion molecules. The I-type lectins are a subset of the immunoglobulin superfamily that are capable of carbohydrate–protein interactions. There are I-type lectins recognizing sialic acids, other sugars and glycosaminoglycans. The occurrence, structure, binding properties and (potential) biological functions of the I-type lectins are reviewed here.