Abstract
The three-dimensional structure of pentameric human serum amyloid P component at high resolution, the first reported for a pentraxin, reveals that the tertiary fold is remarkably similar to that of the legume lectins. Carboxylate and phosphate compounds bind directly to two calcium ions; interactions with a carboxyethylidene ring are mediated by Asn 59 and Gln 148 ligands of the calcium ions. These X-ray results indicate the probable modes of binding of the biologically important ligands, DNA and amyloid fibrils.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Amyloidosis / metabolism
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Binding Sites
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C-Reactive Protein / chemistry
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C-Reactive Protein / metabolism
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Calcium / metabolism
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Computer Graphics
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Crystallography, X-Ray
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DNA / metabolism
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Endopeptidases / metabolism
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Humans
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Ligands
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Methylgalactosides / metabolism
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Models, Molecular
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Molecular Sequence Data
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Phosphatidylethanolamines / metabolism
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Phosphorylcholine / metabolism
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Protein Conformation
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Protein Folding
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Protein Structure, Secondary
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Sequence Alignment
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Serum Amyloid P-Component / chemistry*
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Serum Amyloid P-Component / metabolism
Substances
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Ligands
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Methylgalactosides
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Phosphatidylethanolamines
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Serum Amyloid P-Component
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Phosphorylcholine
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C-Reactive Protein
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DNA
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methyl 4,6-O-(1-carboxyethylidene)galactopyranoside
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Endopeptidases
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Calcium