Abstract
The structure in solution of the second Ig-module fragment of residues 117-208 of NCAM has been determined. Like the first Ig-module of residues 20-116, it belongs to the I set of the immunogloblin superfamily. Module 1 and module 2 interact weakly, and the binding sites of this interaction have been identified. The two-module fragment NCAM(20-208) is a stable dimer. Removal of the charged residues in these sites in NCAM(20-208) abolishes the dimerization. Modeling the dimer of NCAM(20-208) to fit the interactions of these charges produces one coherent binding site for the formation of two antiparallel strands of the first two NCAM modules. This mode of binding could be a major element in trans-cellular interactions in neural cell adhesion.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Substitution
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Binding Sites
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Cell Adhesion
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Crystallization
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Crystallography, X-Ray
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Dimerization
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Disulfides / chemistry
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Immunoglobulins / chemistry
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Models, Molecular
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Molecular Sequence Data
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Neural Cell Adhesion Molecules / chemistry*
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Neural Cell Adhesion Molecules / genetics
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Neural Cell Adhesion Molecules / metabolism
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Neurons / chemistry
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Neurons / cytology
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Neurons / physiology*
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Nuclear Magnetic Resonance, Biomolecular
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Peptide Fragments / chemistry
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Peptide Fragments / genetics
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Peptide Fragments / metabolism*
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Protein Binding
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Protein Conformation
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Protein Structure, Secondary
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Static Electricity
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Thermodynamics
Substances
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Disulfides
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Immunoglobulins
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Neural Cell Adhesion Molecules
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Peptide Fragments