Abstract
The three-dimensional structure of the ligand-binding region of human E-selectin has been determined at 2.0 A resolution. The structure reveals limited contact between the two domains and a coordination of Ca2+ not predicted from other C-type lectins. Structure/function analysis indicates a defined region and specific amino-acid side chains that may be involved in ligand binding. These features of the E-selectin/ligand interaction have important implications for understanding the recruitment of leukocytes to sites of inflammation.
MeSH terms
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Amino Acid Sequence
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Amino Acids / metabolism
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Animals
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CHO Cells
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Carrier Proteins / metabolism
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Cell Adhesion
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Cell Adhesion Molecules / chemistry
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Cell Adhesion Molecules / metabolism*
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Cricetinae
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Crystallography, X-Ray
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E-Selectin
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Epidermal Growth Factor / metabolism*
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Humans
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Lectins / metabolism
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Lewis X Antigen / chemistry
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Ligands
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Mannose-Binding Lectins
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Models, Molecular
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Molecular Sequence Data
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Mutagenesis
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Neutrophils / metabolism
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Rats
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Structure-Activity Relationship
Substances
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Amino Acids
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Carrier Proteins
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Cell Adhesion Molecules
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E-Selectin
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Lectins
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Lewis X Antigen
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Ligands
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Mannose-Binding Lectins
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Epidermal Growth Factor