Abstract
Animal lectins bind to soluble carbohydrates on cell surfaces. The majority of animal lectins are nonenzymatic in activity and usually precipitate glycoconjugates in specific animal cells. It controls protein levels in the blood, modulates cell adhesion to glycoprotein production, and binds soluble extracellular and intracellular glycoproteins. Carbohydrates seen in pathogens that are not recognized by immune system host cells are identified by lectins. Animal lectins have a jelly-like consistency. Animal lectins have a jelly-roll tertiary structure with quaternary connections that vary. P type lectins, C type lectins, I type lectins, Chi lectins, and others are the 15 structural families of animal lectins.
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Abbreviations
- AAA:
-
Anguilla anguilla agglutinin
- CD-MPR:
-
Cation-dependent mannose 6-phosphate receptor
- CI-MPR:
-
Cation-independent mannose 6-phosphate receptor
- CLRD:
-
C type lectin-like receptor domain
- CRD:
-
Carbohydrate recognition domain
- ERAD:
-
Endoplasmic reticulum-associated degradation
- FTLD:
-
F type lectin domain
- IGF2R:
-
Insulin-like growth factor 2 receptor
- LMAN2:
-
Lectin, mannose binding 2
- LRR:
-
Leucine-rich repeats
- MAG:
-
Myelin-associated glycoprotein
- MCFD2:
-
Multicoagulation-factor deficiency 2 protein
- MDCK:
-
Madin-Darby canine kidney
- SBD:
-
Sugar binding domain
- TGN:
-
Trans-Golgi network
- TIM:
-
Triose-phosphate isomerase
- VIP-36:
-
Vesicular integral membrane protein-36
- XCGL:
-
Xenopus oocyte cortical granule lectin
- XEEL:
-
Xenopus embryonic cuticular glycoprotein
- zINTLs:
-
Zebrafish intelectins
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Narayanan, S., Pallan, A.R., Balakrishnan, A., Paul, E.J., Elumalai, P. (2021). Animal Lectin. In: Elumalai, P., Lakshmi, S. (eds) Lectins. Springer, Singapore. https://doi.org/10.1007/978-981-16-7462-4_5
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