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Tandem-repeat lectins: structural and functional insights.
Olvera-Lucio, Francisco H; Riveros-Rosas, Héctor; Quintero-Martínez, Adrián; Hernández-Santoyo, Alejandra.
Afiliación
  • Olvera-Lucio FH; Instituto de Química, Universidad Nacional Autónoma de México, Ciudad de México, Coyoacán 04510, Mexico.
  • Riveros-Rosas H; Depto. Bioquímica, Facultad de Medicina, Universidad Nacional Autónoma de México, Ciudad de México, Coyoacán 04510, Mexico.
  • Quintero-Martínez A; Instituto de Química, Universidad Nacional Autónoma de México, Ciudad de México, Coyoacán 04510, Mexico.
  • Hernández-Santoyo A; Instituto de Química, Universidad Nacional Autónoma de México, Ciudad de México, Coyoacán 04510, Mexico.
Glycobiology ; 34(7)2024 05 26.
Article en En | MEDLINE | ID: mdl-38857376
ABSTRACT
Multivalency in lectins plays a pivotal role in influencing glycan cross-linking, thereby affecting lectin functionality. This multivalency can be achieved through oligomerization, the presence of tandemly repeated carbohydrate recognition domains, or a combination of both. Unlike lectins that rely on multiple factors for the oligomerization of identical monomers, tandem-repeat lectins inherently possess multivalency, independent of this complex process. The repeat domains, although not identical, display slightly distinct specificities within a predetermined geometry, enhancing specificity, affinity, avidity and even oligomerization. Despite the recognition of this structural characteristic in recently discovered lectins by numerous studies, a unified criterion to define tandem-repeat lectins is still necessary. We suggest defining them multivalent lectins with intrachain tandem repeats corresponding to carbohydrate recognition domains, independent of oligomerization. This systematic review examines the folding and phyletic diversity of tandem-repeat lectins and refers to relevant literature. Our study categorizes all lectins with tandemly repeated carbohydrate recognition domains into nine distinct folding classes associated with specific biological functions. Our findings provide a comprehensive description and analysis of tandem-repeat lectins in terms of their functions and structural features. Our exploration of phyletic and functional diversity has revealed previously undocumented tandem-repeat lectins. We propose research directions aimed at enhancing our understanding of the origins of tandem-repeat lectin and fostering the development of medical and biotechnological applications, notably in the design of artificial sugars and neolectins.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Secuencias Repetidas en Tándem / Lectinas Límite: Animals / Humans Idioma: En Revista: Glycobiology Asunto de la revista: BIOQUIMICA Año: 2024 Tipo del documento: Article País de afiliación: México Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Secuencias Repetidas en Tándem / Lectinas Límite: Animals / Humans Idioma: En Revista: Glycobiology Asunto de la revista: BIOQUIMICA Año: 2024 Tipo del documento: Article País de afiliación: México Pais de publicación: Reino Unido