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

Daisuke Kohda, Craig J. Morton, Ashfaq A. Parkar, Hideki Hatanaka, Fuyuhiko M. Inagaki, Iain D. Campbell, Anthony J. Day

Research output: Contribution to journalArticlepeer-review

243 Citations (Scopus)

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 α helices and two antiparallel β 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.

Original languageEnglish
Pages (from-to)767-775
Number of pages9
JournalCell
Volume86
Issue number5
DOIs
Publication statusPublished - Sep 6 1996
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)

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