| Literature DB >> 23178705 |
Nicolas Jonckheere1, Nicolas Skrypek, Frédéric Frénois, Isabelle Van Seuningen.
Abstract
Mucins belong to a heterogeneous family of large O-glycoproteins composed of a long peptidic chain called apomucin on which are linked hundreds of oligosaccharidic chains. Among mucins, membrane-bound mucins are modular proteins and have a structural organization usually containing Pro/Thr/Ser-rich O-glycosylated domains (PTS), EGF-like and SEA domains. Via these modular domains, the membrane-bound mucins participate in cell signalling and cell interaction with their environment in normal and pathological conditions. Moreover, the recent knowledge of these domains and their biological activities led to the development of new therapeutic approaches involving mucins. In this review, we show 3D structures of EGF and SEA domains. We also describe the functional features of the evolutionary conserved domains of membrane-bound mucins and discuss consequences of splice events.Entities:
Mesh:
Substances:
Year: 2012 PMID: 23178705 DOI: 10.1016/j.biochi.2012.11.005
Source DB: PubMed Journal: Biochimie ISSN: 0300-9084 Impact factor: 4.079