TY - JOUR
T1 - Solution structure of the link module
T2 - A hyaluronan-binding domain involved in extracellular matrix stability and cell migration
AU - Kohda, Daisuke
AU - Morton, Craig J.
AU - Parkar, Ashfaq A.
AU - Hatanaka, Hideki
AU - Inagaki, Fuyuhiko M.
AU - Campbell, Iain D.
AU - Day, Anthony J.
N1 - Funding Information:
Correspondence should be addressed to A. J. D. We thank Dr. Jonathan Boyd for assistance with NMR measurements and Drs. Kristy Downing and Caroline Milner for critical reading of the manuscript. This work, A. J. D., and A. A. P. were supported by the Arthritis and Rheumatism Council (grants D0067 and D0086). D. K. acknowledges support from the Japan Society for the Promotion of Science. The Oxford Centre for Molecular Sciences is funded by the Biotechnology and Biological Sciences Research Council (BBSRC), the Engineering and Physical Sciences Research Council, and the Medical Research Council. C. J. M. is funded through a Protein Engineering BBSRC LINK project. I. D. C. acknowledges the Wellcome Trust for support.
PY - 1996/9/6
Y1 - 1996/9/6
N2 - 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.
AB - 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.
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U2 - 10.1016/S0092-8674(00)80151-8
DO - 10.1016/S0092-8674(00)80151-8
M3 - Article
C2 - 8797823
AN - SCOPUS:0030572693
SN - 0092-8674
VL - 86
SP - 767
EP - 775
JO - Cell
JF - Cell
IS - 5
ER -