Solution structure of the link module: a hyaluronan-binding domain involved in extracellular matrix stability and cell migration.
Article Details
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Kohda D, Morton CJ, Parkar AA, Hatanaka H, Inagaki FM, Campbell ID, Day AJ
Solution structure of the link module: a hyaluronan-binding domain involved in extracellular matrix stability and cell migration.
Cell. 1996 Sep 6;86(5):767-75.
- PubMed ID
- 8797823 [ View in PubMed]
- Abstract
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.
DrugBank Data that Cites this Article
- Drug Targets
Drug Target Kind Organism Pharmacological Action Actions Hyaluronic acid Tumor necrosis factor-inducible gene 6 protein Protein Humans UnknownBinderDetails - Polypeptides
Name UniProt ID Tumor necrosis factor-inducible gene 6 protein P98066 Details