Solution structure of the link module: a hyaluronan-binding domain involved in extracellular matrix stability and cell migration.

Article Details

Citation

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
DrugTargetKindOrganismPharmacological ActionActions
Hyaluronic acidTumor necrosis factor-inducible gene 6 proteinProteinHumans
Unknown
Binder
Details
Polypeptides
NameUniProt ID
Tumor necrosis factor-inducible gene 6 proteinP98066Details