Abstract
The three-dimensional structure of the lumenal domain of the lectin-like chaperone calnexin determined to 2.9 A resolution reveals an extended 140 A arm inserted into a beta sandwich structure characteristic of legume lectins. The arm is composed of tandem repeats of two proline-rich sequence motifs which interact with one another in a head-to-tail fashion. Identification of the ligand binding site establishes calnexin as a monovalent lectin, providing insight into the mechanism by which the calnexin family of chaperones interacts with monoglucosylated glycoproteins.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Motifs
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Amino Acid Sequence
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Binding Sites
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Calcium / metabolism
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Calcium-Binding Proteins / chemistry*
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Calcium-Binding Proteins / genetics
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Calcium-Binding Proteins / metabolism
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Calnexin
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Calreticulin
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Crystallography, X-Ray
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Glucose / metabolism
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Membrane Proteins / chemistry
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Models, Molecular
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Molecular Chaperones / chemistry*
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Molecular Chaperones / genetics
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Molecular Chaperones / metabolism
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Molecular Sequence Data
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Protein Conformation
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Protein Folding
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Ribonucleoproteins / chemistry
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Sequence Alignment
Substances
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Calcium-Binding Proteins
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Calreticulin
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Membrane Proteins
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Molecular Chaperones
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Ribonucleoproteins
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Calnexin
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calmegin
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Glucose
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Calcium