Premium
Modeling the Combining Site of the Human Asialoglycoprotein Receptor
Author(s) -
Khier Sharona,
Tolchinsky Sandra,
Lederkremer Gerardo Z.,
Shaanan Boaz
Publication year - 1994
Publication title -
israel journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.908
H-Index - 54
eISSN - 1869-5868
pISSN - 0021-2148
DOI - 10.1002/ijch.199400023
Subject(s) - asialoglycoprotein receptor , chemistry , homology modeling , lectin , binding site , ligand (biochemistry) , receptor , molecular model , mutagenesis , sequence (biology) , biochemistry , computational biology , stereochemistry , biophysics , in vitro , biology , mutation , gene , hepatocyte , enzyme
A model for the carbohydrate recognition domain (CRD) and combining site of the human asialoglycoprotein (ASGP) receptor has been computed on the basis of the close sequence homology with the mannose‐binding lectin (MBP), whose three‐dimensional structure in complex with a ligand has been determined by crystallographic methods (Weis, W.I.; Drickamer, K.; Hendrickson, W.A. Nature 1992, 360: 127). Within the limitations of modeling methods, the model is compatible with data on ligand binding of the family C‐type lectins, of which the MBP and the ASGP receptor are members. The model derived can serve as a guide for designing site‐directed mutagenesis experiments in order to further elucidate the origins of specificity of the ASGP receptor toward galactose. In particular, the model focuses attention on the possible role of position 207 (MBP sequence numbering) in promoting galactose binding.