Abstract
The selectins are a family of cellβadhesion proteins that mediate the rolling of leukocytes on activated endothelial cells through the recognition of the carbohydrate epitope sialyl Lewis^x^ (sLe^x^). Control of the leukocyteβendothelial cell adhesion process may prove useful in cases where excess recruitment of leukocytes can contribute to acute diseases such as stroke and reperfusion injury and chronic diseases such as psoriasis and rheumatoid arthritis. The development of molecules that block the interactions between sLe^x^ and the selectins has become an active area of research. In this review, we will highlight the various approaches taken toward the development of sLe^x^ mimetics as antagonists of Eβ and Pβselectin, including the use of structural information about the selectins and their interactions with sLe^x^ that have been revealed through the use of NMR, protein crystallography and molecular modeling. Β© 2002 Wiley Periodicals, Inc. Med Res Rev, 22, No. 6, 566β601, 2002; Published online in Wiley InterScience (www.interscience.wiley.com). DOI 10.1002/med.10018