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| | Pfam 20.0 : Kringle (Site not responding. Last check: 2007-10-25) |
 | | Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta. |
 | | Kringle domains are believed to play a role in binding mediators (e.g., membranes, other proteins or phospholipids), and in the regulation of proteolytic activity PUBMED:3886654, PUBMED:6373375, PUBMED:2157850. |
 | | Kringle domains PUBMED:3131537, PUBMED:3891096, PUBMED:1879523 are characterised by a triple loop, 3-disulphide bridge structure, whose conformation is defined by a number of hydrogen bonds and small pieces of anti-parallel beta-sheet. |
| pfam.wustl.edu /cgi-bin/getdesc?name=Kringle (118 words) |
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