Structural motif screening reveals a novel,conserved carbohydrate-binding surface in the pathogenesis-related protein PR-5d |
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| Authors: | Andrew C Doxey Zhenyu Cheng Barbara A Moffatt Brendan J McConkey |
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| Affiliation: | (1) Department of Biology, University of Waterloo, 200 University Avenue West, N2L 3G1 Waterloo, Ontario, Canada;(2) Department of Developmental Biology, Stanford University, 94305 Stanford, CA, USA |
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| Abstract: | Background Aromatic amino acids play a critical role in protein-glycan interactions. Clusters of surface aromatic residues and their features may therefore be useful in distinguishing glycan-binding sites as well as predicting novel glycan-binding proteins. In this work, a structural bioinformatics approach was used to screen the Protein Data Bank (PDB) for coplanar aromatic motifs similar to those found in known glycan-binding proteins. |
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