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.
Kohda
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Department of Biochemistry Oxford Centre for Molecular Sciences University of Oxford, United Kingdom.
Morton
C J
CJ
Parkar
A A
AA
Hatanaka
H
H
Inagaki
F M
FM
Campbell
I D
ID
Day
A J
AJ
D000595:Amino Acid Sequence; D001665:Binding Sites; D050260:Carbohydrate Metabolism; D015815:Cell Adhesion Molecules / Q000737:chemistry* / Q000378:metabolism; D002465:Cell Movement; D019040:E-Selectin / Q000737:chemistry; D005109:Extracellular Matrix / Q000502:physiology; D006801:Humans; D006820:Hyaluronic Acid / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid; D012996:Solutions
D015815:Cell Adhesion Molecules; D019040:E-Selectin; D012996:Solutions; C072273:TNFAIP6 protein, human; D006820:Hyaluronic Acid