Abstract
The work presented here is aimed at suggesting plausible hypotheses for functional oligomeric forms of the human asialoglycoprotein receptor (ASGP-R), by applying a combination of different computational techniques. The functional ASGP-R is a hetero-oligomer, that comprises of several subunits of two different kinds (H1 and H2), which are highly homologous. Its stoichiometry is still unknown. An articulated step-wise modeling protocol was used in order to build the receptor model in a minimal oligomeric form, necessary for it to bind multi-antennary carbohydrate ligands. The ultimate target of the study is to contribute to increasing the knowledge of interactions between the human ASGP-R and carbohydrate ligands, at the molecular level, pertinent to applications in the field of hepatic tissue engineering.
Highlights
The human asialoglycoprotein receptor (ASGP-R), called hepatic lectin, is a C-type lectin of hepatocytes that recognizes desialylated glycoproteins for endocytosis and lysosomal degradation
Specificity and affinity of ligand binding are accomplished by the simultaneous interaction of at least three terminal ligand residues with three carbohydrate recognition domains (CRDs) [1]
In this work we propose a step-wise procedure for building a minimum assessed oligomeric structure, i.e., a H1-H1-H2 trimer
Summary
The human asialoglycoprotein receptor (ASGP-R), called hepatic lectin, is a C-type (calcium dependent) lectin of hepatocytes that recognizes desialylated glycoproteins for endocytosis and lysosomal degradation. It has been largely studied in recent years [1,2,3,4,5,6,7,8,9,10] due to its possible role in a wide range of practical applications in human health. The functional form of the human receptor is a noncovalent hetero-oligomer composed of two homologous subunits, generically called H1 and H2 [2] Simultaneous expression of both subunits was found to be necessary to generate high affinity binding sites.
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