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Modelling the carbohydrate recognition domain of human E‐selectin
Author(s) -
Mills Alan
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80026-q
Subject(s) - tetrasaccharide , e selectin , chemistry , lectin , glycoprotein , mannose , ligand (biochemistry) , homology (biology) , binding domain , biophysics , biochemistry , binding site , stereochemistry , computational biology , cell adhesion , biology , amino acid , polysaccharide , cell , receptor
The three‐dimensional structure of the carbohydrate recognition domain of the human E‐selectin endothelial‐leucocyte adhesion molecule (ELAM‐1) was modelled on the basis of the recently determined X‐ray crystallographic structure of the homologous domain found in the rat mannose‐binding protein. The EGF‐like module, which is contiguous to the E‐selectin lectin domain, and which is also involved in binding the tetrasaccharide ligand, was modelled on the recently determined NMR structure of the EGF‐like module of human factor IX. The rule‐based homology modelling procedures developed at Birkbeck and encoded in the program COMPOSER were used. The model of the two domains combined is discussed in terms of cation and ligand binding.