Solution structure of the link module: a hyaluronan-binding domain involved in extracellular matrix stability and cell migration.
Link modules are hyaluronan-binding domains found in proteins involved in the assembly of extracellular matrix, cell adhesion, and migration. The solution structure of the Link module from human TSG-6 was determined and found to consist of two alpha helices and two antiparallel beta sheets arranged around a large hydrophobic core. ... This defines the consensus fold for the Link module superfamily, which includes CD44, cartilage link protein, and aggrecan. The TSG-6 Link module was shown to interact with hyaluronan, and a putative binding surface was identified on the structure. A structural database search revealed close similarity between the Link module and the C-type lectin domain, with the predicted hyaluronan-binding site at an analogous position to the carbohydrate-binding pocket in E-selectin.
Mesh Terms:
Amino Acid Sequence, Binding Sites, Carbohydrate Metabolism, Cell Adhesion Molecules, Cell Movement, E-Selectin, Extracellular Matrix, Humans, Hyaluronic Acid, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Folding, Protein Structure, Secondary, Sequence Homology, Amino Acid, Solutions
Amino Acid Sequence, Binding Sites, Carbohydrate Metabolism, Cell Adhesion Molecules, Cell Movement, E-Selectin, Extracellular Matrix, Humans, Hyaluronic Acid, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Folding, Protein Structure, Secondary, Sequence Homology, Amino Acid, Solutions
Cell
Date: Sep. 06, 1996
PubMed ID: 8797823
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