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Title
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Introduction of selectin-like binding specificity into a homologous mannose-binding protein.
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Authors
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O.Blanck,
S.T.Iobst,
C.Gabel,
K.Drickamer.
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Ref.
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J Biol Chem, 1996,
271,
7289-7292.
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PubMed id
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Abstract
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The structures of the ligand-binding C-type carbohydrate-recognition domains of
selectin cell adhesion molecules and of mannose-binding proteins (MBPs) are
similar to each other even though these proteins bind very different
carbohydrate ligands. Our current understanding of ligand binding by E-selectin
is based on structural studies of unliganded E-selectin and of MBP-carbohydrate
complexes, combined with results from mutagenesis of E-selectin. Five regions of
E-selectin that differ in sequence from the corresponding regions of MBP have
been introduced into the carbohydrate-recognition domain of MBP. Four of the
changes have little effect on ligand binding. Insertion of one stretch of
positively charged amino acids alters the sugar binding selectivity of the
domain so that it now binds HL-60 cells and serum albumin derivatized with
sialyl-Lewis X tetrasaccharide, thus mimicking the properties of E-selectin.
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