LamBLaminin B domain
|SMART accession number:||SM00281|
|Interpro abstract (IPR018031):|
Laminins represent a distinct family of extracellular matrix proteins present only in basement membranes in almost every animal tissue. They are heterotrimeric molecules composed of alpha, beta and gamma subunits (formerly A, B1, and B2, respectively [(PUBMED:7921537)]) and form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains, [(PUBMED:2404817), (PUBMED:7827749)]. Most of the globular domains of the short arms correspond to one of two different motifs, the 200-residue laminin N-terminal (domain VI) (LN) module and the 250-residue laminin domain IV (L4) module [(PUBMED:8615779)]. All alpha chains share a unique C-terminal G domain which consists of five laminin G modules. The laminins can self-assemble, bind to other matrix macromolecules, and have unique and shared cell interactions mediated by integrins, dystroglycan, and other receptors. There are at least 14 laminin isoforms that regulate a variety of cellular functions including cell adhesion, migration, proliferation, signalling and differentiation [(PUBMED:9758133), (PUBMED:7827749), (PUBMED:11054872)].
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- Evolution (species in which this domain is found)
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