Members of this family adopt a fold similar to other EGFdomains, with a flat major and a twisted minor beta sheet.Disulphide pairing, however, is not of the usual 1-3, 2-4, 5-6type; rather 1-2, 3-4, 5-6 pairing is found. Its extended majorsheet (strands beta-2 and beta-3 and the connecting loop)projects into thrombin's active site groove. This domain isrequired for interaction of thrombomodulin with thrombin, andsubsequent activation of protein-C [1]. Thrombomodulin like fifth domain, EGF-like Tme5_EGF_like