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. doi: 10.1016/s0092-8674(00)80151-8.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Carbohydrate Metabolism
  • Cell Adhesion Molecules / chemistry*
  • Cell Adhesion Molecules / metabolism
  • Cell Movement
  • E-Selectin / chemistry
  • Extracellular Matrix / physiology
  • Humans
  • Hyaluronic Acid / metabolism*
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Binding
  • Protein Folding
  • Protein Structure, Secondary*
  • Sequence Homology, Amino Acid
  • Solutions

Substances

  • Cell Adhesion Molecules
  • E-Selectin
  • Solutions
  • TNFAIP6 protein, human
  • Hyaluronic Acid

Associated data

  • GENBANK/UNKNOWN